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{{short description|English biochemist and academic}}
{{EngvarB|date=August 2017}}
{{EngvarB|date=August 2017}}
{{Use dmy dates|date=August 2017}}
{{Use dmy dates|date=August 2017}}
{{For|other people called Jane Clarke|Jane Clarke (disambiguation){{!}}Jane Clarke}}
{{Infobox scientist
{{Infobox scientist
| name = Jane Clarke
| name = Jane Clarke
| birth_name = Jane Morgan<ref name=whoswho/>
| birth_name = Jane Morgan
| image = Professor Jane Clarke FMedSci FRS.jpg
| image = Professor Jane Clarke FMedSci FRS.jpg
| image_size =
| image_size =
| alt =
| alt =
| caption = Jane Clarke at the [[Royal Society]] admissions day in London, July 2015
| caption = Clarke in 2015
| birth_date = {{Birth date and age|df=yes|1950|09|10}}<ref name=whoswho>{{Who's Who | surname = CLARKE | othernames = Prof. Jane | id = U279617 | volume = 2015 | edition = online [[Oxford University Press]]}} {{subscription required}}</ref>
| birth_date = {{Birth date and age|df=yes|1950|09|10}}
| birth_place = London
| birth_place = [[London]], England
| other_names =
| other_names =
| residence =
| residence =
| citizenship =
| citizenship =
| nationality =
| nationality =
| fields = {{Plainlist|
| fields = {{Plainlist|
* [[Biophysics]]
* [[Biophysics]]
Line 20: Line 20:
* [[Protein folding]]}}
* [[Protein folding]]}}
| workplaces = {{Plainlist|
| workplaces = {{Plainlist|
* [[University of Cambridge]]
* [[Trinity Hall, Cambridge]]
* [[Wolfson College, Cambridge]]}}
* [[Centre for Protein Engineering]]
| patrons =
* [[Northumberland Park Community School]]}}
| honorific_suffix = {{Post-nominals|country=GBR|FRS|FRSC|FMedSci|size=100%}}
| patrons =
| alma_mater = {{Plainlist|
| alma_mater = {{Plainlist|
* [[University of York]] (BSc)
* [[University of York]]
* [[Georgia Institute of Technology]] (MSc)
* [[Georgia Institute of Technology]]
* [[University of Cambridge]] (PGCE, PhD)}}
* [[University of Cambridge]]<ref name=whoswho/>}}
| thesis_title = Studies of disulphide mutants of barnase
| thesis_title = Studies of Disulphide Mutants of Barnase
| thesis_url = http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.318014
| thesis_url = http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.318014
| thesis_year = 1993
| thesis_year = 1993
| doctoral_advisor = [[Alan Fersht]]<ref name=fersht>{{cite web|archiveurl=https://web.archive.org/web/20150324163357/http://www.cam.ac.uk/women-at-cambridge/profiles/jane-clarke|title=Women at Cambridge: Jane Clarke|url=http://www.cam.ac.uk/women-at-cambridge/profiles/jane-clarke|publisher=University of Cambridge|archivedate=2015-03-24}}</ref>
| doctoral_advisor = [[Alan Fersht]]<ref name=fersht>{{cite web|archive-url=https://web.archive.org/web/20150324163357/http://www.cam.ac.uk/women-at-cambridge/profiles/jane-clarke|author=Anon|year=2015|title=Women at Cambridge: Jane Clarke|url=http://www.cam.ac.uk/women-at-cambridge/profiles/jane-clarke|publisher=University of Cambridge|archive-date=2015-03-24}}</ref><ref name=janephd/>
| academic_advisors =
| academic_advisors =
| doctoral_students =
| doctoral_students =
| notable_students = {{Plainlist|
| notable_students =
| known_for =
* Sarah Batey<ref>{{cite thesis|degree=PhD|publisher=University of Cambridge|title=Folding in a multi-domain protein|first= Sarah|last=Batey|year=2005|url=http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.614980}}</ref>
| influences =
* Robert Best<ref>{{cite thesis|degree=PhD|publisher=University of Cambridge|title=High resolution studies of protein folding and dynamics|first= Robert.|last=Best|year=2003|url=http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.596604}}</ref>
| influenced =
* Kate Billings<ref>{{cite thesis|degree=PhD|publisher=University of Cambridge|title=Studies on core-swapped fibronectin type III domains|first= Kate S.|last=Billings|year=2007|url=http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.596637}}</ref>
| awards = US Genomics Award (2010)
* Ernesto Cota<ref>{{cite thesis|degree=PhD|publisher=University of Cambridge|title=Studies on the folding of the tenth fnIII domain of the human fibronectin|first= Ernesto|last=Cota-Segura|year=2000|url=http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.621658}}</ref>
* Julia Forman<ref>{{cite thesis|degree=PhD|publisher=University of Cambridge|title=Biophysical investigations of PKD domains: mechanosensation and pathogenesis|first= Julia R.|last=Forman|year=2006|url=http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.599119}}</ref><ref name=forman/>
* Susan Fowler<ref>{{cite thesis|degree=PhD|publisher=University of Cambridge|title=Folding studies on an immunoglobulin domain using chemical and mechanical methods|first= Susan B.|last=Fowler|year=2002|url=http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.599147}}</ref>
* Christian Geierhaas<ref>{{cite thesis|degree=PhD|publisher=University of Cambridge|title=Computational studies of protein folding|first= Christian D.|last=Geierhaas|year=2006|url=http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.613877}}</ref>
* Stephan Hamill<ref>{{cite thesis|degree=PhD|publisher=University of Cambridge|title=Folding and evolution of the immunoglobulin-like superfold|first= Stephan. J.|last=Hamill|year=2000|url=http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.603613}}</ref>
* Stephanie Hill<ref name=personnel>{{cite web|archiveurl=https://web.archive.org/web/20130227112037/http://www-clarke.ch.cam.ac.uk/Personnel.php|url=http://www-clarke.ch.cam.ac.uk/Personnel.php|title=Current and former members of Jane Clarke's laboratory|publisher=University of Cambridge|archivedate=2013-02-27}}</ref>
* Mike Hurley<ref>{{cite thesis|degree=PhD|publisher=University of Cambridge|title=Analysis and prediction of the protein folding nucleus using computational and experimental techniques|first= Mike G.|last=Hurley|year=2007|url=http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.604825}}</ref>
* Sean Ng<ref>{{cite thesis|degree=PhD|publisher=University of Cambridge|title=Biophysical studies of mechanical proteins|first= Sean Pin|last=Ng|year=2006|url=http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.613990}}</ref>
* Tina Perica<ref name=periciaphd>{{cite thesis |degree=PhD|first=Tina|last=Perica|title=Evolutionary and structural dynamics of protein complexes |publisher=University of Cambridge|year=2013|url=http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.607933}}</ref><ref name=perica/>
* Lucy Randles<ref>{{cite thesis|degree=PhD|publisher=University of Cambridge|title=Studies of multidomain proteins: effects of force and mutation|first= Lucy Gaynor|last=Randles|year=2008|url=http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.611887}}</ref><ref name=randles1/><ref name=randles2/>
* Joseph Rogers<ref name=personnel/><ref name=rogers/>
* Madeleine Ross<ref name=personnel/>
* Ross Rounsevell<ref>{{cite thesis|degree=PhD|publisher=University of Cambridge|title=Mutational analysis of the mechanical unfolding pathway of TNfn3|first= Ross William Stanley|last=Rounsevell|year=2005|url=http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.615004|oclc=890158123}}</ref>
* Kathryn Scott<ref>{{cite thesis|degree=PhD|publisher=University of Cambridge|title=Biophysical studies of multidomain proteins|first= Kathryn Anne|last=Scott|year=2004|url=http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.616134}}</ref>
* Beth Wensley<ref>{{cite thesis|degree=PhD|publisher=University of Cambridge|title=Investigating the folding of a three-helix bundle protein family|first= Beth Gillian|last=Wensley|year=2009|url=http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.611848}}</ref>}}
| known_for =
| influences =
| influenced =
| awards = {{Plainlist|
* [[Fellow of the Royal Society|FRS]] (2015)
* [[Fellow of the Royal Society of Chemistry|FRSC]] (2013)
* [[FMedSci]] (2013)
* US Genomics Award (2010)}}
| website = {{URL|www-clarke.ch.cam.ac.uk}}
| website = {{URL|www-clarke.ch.cam.ac.uk}}
| footnotes =
| spouse = {{marriage|Christopher Clarke|1973}}
}}
| spouse = {{marriage|Christopher Clarke|1973}}<ref name=whoswho/>
| children = one son, one daughter<ref name=whoswho/>}}


'''Jane Clarke''', {{Post-nominals|country=GBR|FRS|FRSC|FMedSci|size=100%|sep=,}} (née '''Morgan'''; born 10 September 1950) is a British [[biochemist]] and academic. Since October 2017, she has been [[Master (college)|President]] of [[Wolfson College, Cambridge]].<ref>{{cite web|title=Introducing our new President: Professor Jane Clarke FMedSci FRS|url=https://www.wolfson.cam.ac.uk/node/38556|website=Wolfson College|publisher=University of Cambridge|accessdate=26 October 2017}}</ref> She is also Professor of [[Molecular Biophysics]], a [[Wellcome Trust]] Senior Research Fellow<ref name=wt/> in the [[Department of Chemistry, University of Cambridge|Department of Chemistry]] at the [[University of Cambridge]]. She was previously a Fellow of [[Trinity Hall, Cambridge]].<ref name=jc162>{{cite web|archiveurl=https://web.archive.org/web/20140228221755/http://www.ch.cam.ac.uk/person/jc162|url=http://www.ch.cam.ac.uk/person/jc162|title=Professor Jane Clarke FMedSci, Biophysical and structural studies of protein folding|archivedate=2014-02-28|publisher=University of Cambridge}}</ref><ref name=scopus>{{Scopus|id=7403197330}}</ref>
'''Jane Clarke''' (née '''Morgan'''; born 1950) is a British [[biochemist]] and academic. Since October 2017, she has served as [[Master (college)|President]] of [[Wolfson College, Cambridge]].<ref name="University of Cambridge">{{cite web|title=Introducing our new President: Professor Jane Clarke FMedSci FRS|url=https://www.wolfson.cam.ac.uk/node/38556|website=Wolfson College|publisher=University of Cambridge|access-date=26 October 2017}}{{Dead link|date=September 2024 |bot=InternetArchiveBot |fix-attempted=yes }}</ref> She is also Professor of [[Molecular Biophysics]], a [[Wellcome Trust]] Senior [[Research Fellow]]<ref name=wt/> in the [[Department of Chemistry, University of Cambridge|Department of Chemistry]] at the [[University of Cambridge]]. She was previously a [[Fellow]] of [[Trinity Hall, Cambridge]].<ref name=jc162>{{cite web|archive-url=https://web.archive.org/web/20140228221755/http://www.ch.cam.ac.uk/person/jc162|url=http://www.ch.cam.ac.uk/person/jc162|title=Professor Jane Clarke FMedSci, Biophysical and structural studies of protein folding|archive-date=2014-02-28|publisher=University of Cambridge}}</ref><ref name=scopus>{{Scopus id}}</ref><ref name=orcid>{{ORCID}}</ref> In 2023, she was elected to the [[National Academy of Sciences]].<ref>{{cite web | url=http://www.nasonline.org/news-and-multimedia/news/2023-nas-election.html | title=2023 NAS Election }}</ref>


==Education and career==
==Early life and education==
Clarke was educated at the [[University of York]] where she graduated with a [[British undergraduate degree classification|first class honours degree]] in [[Biochemistry]] in 1972.<ref name=whoswho/> She went on to study for a [[Postgraduate Certificate in Education|Postgraduate Certificate in Education (PGCE)]] at the [[University of Cambridge]] in 1973.<ref name=whoswho/> Clarke was a science teacher in several secondary schools, and a Head of Science at [[Northumberland Park Community School|Northumberland Park School, Tottenham]] from 1973 to 1986.
Clarke was born Jane Morgan in [[London]] on 10 September 1950. She was educated at the [[University of York]] where she graduated with a [[British undergraduate degree classification|first-class honours degree]] in [[biochemistry]] in 1972.<ref name=whoswho>{{Who's Who | title=Clarke, Prof. Jane | id = U279617 | year = 2015 | author=Anon| doi=10.1093/ww/9780199540884.013.U279617| edition = online [[Oxford University Press]]}}</ref> She went on to study for a [[Postgraduate Certificate in Education]] (PGCE) at the [[University of Cambridge]] in 1973.<ref name=whoswho/> Clarke was a science teacher in several secondary schools, and a Head of Science at [[Duke's Aldridge Academy|Northumberland Park School, Tottenham]], from 1973 to 1986.<ref name="Clarke27 April 2021" />


She returned to research, gaining a Master of Science degree in Applied Biology in 1990 from the [[Georgia Institute of Technology]] and a PhD in 1993 for investigations of [[Barnase|Bacterial Ribonuclease (Barnase)]] from the [[University of Cambridge]] supervised by [[Alan Fersht]].<ref name=fersht/><ref name=phd>{{cite thesis |degree=PhD |first=Jane|last=Clarke |title=Studies of disulphide mutants of barnase |publisher=University of Cambridge |year=1993 |url=http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.318014|oclc=53666398}}</ref><ref name=fersht1/>
Clarke married Christopher Clarke in 1973 with whom she would go on to have one son and one daughter.<ref name=whoswho/> He obtained a job in the United States and the family moved there. Since Clarke was unable to work as a teacher, through not having appropriate qualifications she decided to update her scientific knowledge through a [[Master of Science]] degree in applied biology, awarded in 1990 from the [[Georgia Institute of Technology]]. This experience made her decide to seek a career in research related to proteins.<ref name="Clarke27 April 2021" /> She was subsequently awarded a [[Doctor of Philosophy]] degree in 1993 for investigations of [[Barnase|Bacterial Ribonuclease (Barnase)]] from the [[University of Cambridge]] supervised by [[Alan Fersht]].<ref name=fersht/><ref name=janephd>{{cite thesis |degree=PhD |first=Jane |last=Clarke |title=Studies of disulphide mutants of barnase |publisher=University of Cambridge |year=1993 |id={{EThOS|uk.bl.ethos.318014}} |oclc=53666398 |url=https://copac.jisc.ac.uk/id/9551412?style=html |website=jisc.ac.uk |access-date=22 December 2018 |archive-date=22 December 2018 |archive-url=https://web.archive.org/web/20181222125453/https://copac.jisc.ac.uk/id/9551412?style=html |url-status=dead }}</ref><ref name=fersht1>{{Cite journal

Clarke was appointed a Wellcome Trust Senior Research Fellow in 2001, a Professor of Molecular Biophysics in 2009 and a Fellow of [[Trinity Hall, Cambridge]] in 2010.<ref name=whoswho/>

==Research==
Clarke's research investigates [[protein folding]],<ref name=research>{{cite web|archiveurl=https://web.archive.org/web/20130126033140/http://www-clarke.ch.cam.ac.uk/Research.php|url=http://www-clarke.ch.cam.ac.uk/Research.php|publisher=University of Cambridge|archivedate=2013-01-26|title=Jane Clarke Laboratory Research Areas}}</ref> in particular:
# Studies of [[Protein family|Structurally Related Proteins]]
# [[Protein domain|Multidomain Proteins]]: Effects of Sequence on Folding and Misfolding
# Folding and Assembly: [[Intrinsically disordered proteins]]

Clarke's research has been funded by the [[Wellcome Trust]],<ref name=wt>{{cite web|archiveurl=https://web.archive.org/web/20140918043150/http://www.wellcome.ac.uk/Funding/Biomedical-science/Funded-projects/Awards-made/Wellcome-Fellows/WTD003235.htm|title=Senior Research Fellows in Basic Biomedical Science|publisher=Wellcome Trust|archivedate=2014-09-18|url=http://www.wellcome.ac.uk/Funding/Biomedical-science/Funded-projects/Awards-made/Wellcome-Fellows/WTD003235.htm}}</ref> [[Medical Research Council (United Kingdom)|Medical Research Council (MRC)]] and the [[Biotechnology and Biological Sciences Research Council|Biotechnology and Biological Sciences Research Council (BBSRC)]]<ref name=gtr>{{cite web|archiveurl=https://web.archive.org/web/20150413124239/http://gtr.rcuk.ac.uk/person/2F243482-207E-4F42-A2F5-77440C7E7154|title=UK Government Grants awarded Jane Clarke|publisher=[[Research Councils UK]]|url=http://gtr.rcuk.ac.uk/person/2F243482-207E-4F42-A2F5-77440C7E7154|archivedate=2015-04-13}}</ref> and has been published in leading [[peer review]]ed [[scientific journal]]s including ''[[Biochemistry (journal)|Biochemistry]]'',<ref name=fersht1>{{Cite journal
| pmid = 8476861
| pmid = 8476861
| year = 1993
| year = 1993
| author1 = Clarke
| last1 = Clarke
| first1 = J
| first1 = J
| authorlink1 = Jane Clarke (scientist)
| author-link1 = Jane Clarke (scientist)
| title = Engineered disulfide bonds as probes of the folding pathway of barnase: Increasing the stability of proteins against the rate of denaturation
| title = Engineered disulfide bonds as probes of the folding pathway of barnase: Increasing the stability of proteins against the rate of denaturation
| journal = Biochemistry
| journal = Biochemistry
Line 93: Line 60:
| pages = 4322–9
| pages = 4322–9
| last2 = Fersht
| last2 = Fersht
| first2 = A. R. | authorlink2 = Alan Fersht
| first2 = A. R. | author-link2 = Alan Fersht
| doi=10.1021/bi00067a022
| doi=10.1021/bi00067a022
}}</ref> ''[[Structure (journal)|Structure]]'',<ref>{{Cite journal | doi = 10.1016/S0969-2126(99)80181-6| title = Folding studies of immunoglobulin-like β-sandwich proteins suggest that they share a common folding pathway| journal = Structure| volume = 7| issue = 9| pages = 1145–1153| year = 1999| last1 = Clarke | first1 = J. | last2 = Cota | first2 = E. | last3 = Fowler | first3 = S. B. | last4 = Hamill | first4 = S. J. }}</ref> the ''[[Journal of Biological Chemistry]]'', the ''[[Biophysical Journal]]'',<ref name=randles1>{{Cite journal
| pmid = 17890397
| pmc = 2157218
| year = 2008
| author1 = Randles
| first1 = L. G.
| title = Distinguishing specific and nonspecific interdomain interactions in multidomain proteins
| journal = Biophysical Journal
| volume = 94
| issue = 2
| pages = 622–8
| last2 = Batey
| first2 = S
| last3 = Steward
| first3 = A
| last4 = Clarke
| first4 = J
| doi = 10.1529/biophysj.107.119123
}}</ref><ref name=randles2>{{Cite journal
| pmid = 17085494
| pmc = 1751415
| year = 2007
| author1 = Randles
| first1 = L. G.
| title = Spectrin domains lose cooperativity in forced unfolding
| journal = Biophysical Journal
| volume = 92
| issue = 2
| pages = 571–7
| last2 = Rounsevell
| first2 = R. W.
| last3 = Clarke
| first3 = J
| doi = 10.1529/biophysj.106.093690
}}</ref><ref>{{Cite journal
| pmid = 23200054
| pmc = 3512043
| year = 2012
| author1 = Shammas
| first1 = S. L.
| title = Slow, reversible, coupled folding and binding of the spectrin tetramerization domain
| journal = Biophysical Journal
| volume = 103
| issue = 10
| pages = 2203–14
| last2 = Rogers
| first2 = J. M.
| last3 = Hill
| first3 = S. A.
| last4 = Clarke
| first4 = J
| doi = 10.1016/j.bpj.2012.10.012
}}</ref><ref>{{Cite journal
| pmid = 16603501
| pmc = 1479071
| year = 2006
| author1 = Geierhaas
| first1 = C. D.
| title = Structural comparison of the two alternative transition states for folding of TI I27
| journal = Biophysical Journal
| volume = 91
| issue = 1
| pages = 263–75
| last2 = Best
| first2 = R. B.
| last3 = Paci
| first3 = E
| last4 = Vendruscolo
| first4 = M
| last5 = Clarke
| first5 = J
| doi = 10.1529/biophysj.105.077057
}}</ref><ref>{{Cite journal
| pmid = 16387757
| pmc = 1386790
| year = 2006
| author1 = Batey
| first1 = S
| title = Complex folding kinetics of a multidomain protein
| journal = Biophysical Journal
| volume = 90
| issue = 6
| pages = 2120–30
| last2 = Scott
| first2 = K. A.
| last3 = Clarke
| first3 = J
| doi = 10.1529/biophysj.105.072710
}}</ref><ref>{{Cite journal
| pmid = 11566804
| pmc = 1301705
| year = 2001
| author1 = Best
| first1 = R. B.
| title = Can non-mechanical proteins withstand force? Stretching barnase by atomic force microscopy and molecular dynamics simulation
| journal = Biophysical Journal
| volume = 81
| issue = 4
| pages = 2344–56
| last2 = Li
| first2 = B
| last3 = Steward
| first3 = A
| last4 = Daggett
| first4 = V
| last5 = Clarke
| first5 = J
| doi = 10.1016/S0006-3495(01)75881-X
}}</ref><ref>{{Cite journal
| pmid = 15613637
| pmc = 1305254
| year = 2005
| author1 = Rounsevell
| first1 = R. W.
| title = Biophysical investigations of engineered polyproteins: Implications for force data
| journal = Biophysical Journal
| volume = 88
| issue = 3
| pages = 2022–9
| last2 = Steward
| first2 = A
| last3 = Clarke
| first3 = J
| doi = 10.1529/biophysj.104.053744
}}</ref> ''[[Nature (journal)|Nature]]'',<ref>{{Cite journal
| doi = 10.1038/nature04195
| pmid = 16341018
| title = The importance of sequence diversity in the aggregation and evolution of proteins
| journal = [[Nature (journal)|Nature]]
| volume = 438
| issue = 7069
| pages = 878–81
| year = 2005
| last1 = Wright | first1 = C. F.
| last2 = Teichmann | first2 = S. A.
| authorlink2 = Sarah Teichmann
| last3 = Clarke | first3 = J. | authorlink3 = Jane Clarke (scientist)
| last4 = Dobson | first4 = C. M.
| authorlink4 = Chris Dobson
}}</ref> ''[[Science (journal)|Science]]'',<ref name=perica>{{Cite journal
| pmid = 25525255
| pmc = 4337988
| year = 2014
| author1 = Perica
| first1 = T
| title = Evolution of oligomeric state through allosteric pathways that mimic ligand binding
| journal = Science
| volume = 346
| issue = 6216
| pages = 1254346
| last2 = Kondo
| first2 = Y
| last3 = Tiwari
| first3 = S. P.
| last4 = McLaughlin
| first4 = S. H.
| last5 = Kemplen
| first5 = K. R.
| last6 = Zhang
| first6 = X
| last7 = Steward
| first7 = A
| last8 = Reuter
| first8 = N
| last9 = Clarke
| first9 = J
| authorlink9 = Jane Clarke (scientist)
| last10 = Teichmann
| first10 = S. A. | authorlink10 = Sarah Teichmann
| doi = 10.1126/science.1254346
}}</ref> ''[[Proceedings of the National Academy of Sciences of the United States of America|PNAS]]'',<ref>{{Cite journal
| pmid = 10097099
| pmc = 22356
| year = 1999
| author1 = Carrion-Vazquez
| first1 = M
| title = Mechanical and chemical unfolding of a single protein: A comparison
| journal = Proceedings of the National Academy of Sciences of the United States of America
| volume = 96
| issue = 7
| pages = 3694–9
| last2 = Oberhauser
| first2 = A. F.
| last3 = Fowler
| first3 = S. B.
| last4 = Marszalek
| first4 = P. E.
| last5 = Broedel
| first5 = S. E.
| last6 = Clarke
| first6 = J
| last7 = Fernandez
| first7 = J. M.
| doi=10.1073/pnas.96.7.3694
}} {{open access}}</ref> the ''[[Journal of the American Chemical Society]]'',<ref name=rogers>{{Cite journal
| pmid = 24654952
| pmc = 4017604
| year = 2014
| author1 = Rogers
| first1 = J. M.
| title = Coupled folding and binding of the disordered protein PUMA does not require particular residual structure
| journal = Journal of the American Chemical Society
| volume = 136
| issue = 14
| pages = 5197–200
| last2 = Wong
| first2 = C. T.
| last3 = Clarke
| first3 = J
| doi = 10.1021/ja4125065
}}</ref><ref>{{Cite journal
| pmid = 23510407
| pmc = 3759167
| year = 2013
| author1 = Borgia
| first1 = M. B.
| title = A mechanistic model for amorphous protein aggregation of immunoglobulin-like domains
| journal = Journal of the American Chemical Society
| volume = 135
| issue = 17
| pages = 6456–64
| last2 = Nickson
| first2 = A. A.
| last3 = Clarke
| first3 = J
| last4 = Hounslow
| first4 = M. J.
| doi = 10.1021/ja308852b
}}</ref><ref>{{Cite journal
| pmid = 23301700
| pmc = 3776562
| year = 2013
| author1 = Rogers
| first1 = J. M.
| title = Folding and binding of an intrinsically disordered protein: Fast, but not 'diffusion-limited'
| journal = Journal of the American Chemical Society
| volume = 135
| issue = 4
| pages = 1415–22
| last2 = Steward
| first2 = A
| last3 = Clarke
| first3 = J
| doi = 10.1021/ja309527h
}}</ref><ref>{{Cite journal
| pmid = 15212494
| year = 2004
| author1 = Best
| first1 = R. B.
| title = The origin of protein sidechain order parameter distributions
| journal = Journal of the American Chemical Society
| volume = 126
| issue = 25
| pages = 7734–5
| last2 = Clarke
| first2 = J | authorlink2 = Jane Clarke (scientist)
| last3 = Karplus
| first3 = M | authorlink3 = Martin Karplus
| doi = 10.1021/ja049078w
}}</ref> ''[[Current Opinion (Elsevier)|Current Opinion Structural Biology]]''<ref name=forman>{{Cite journal
| pmid = 17251000
| year = 2007
| author1 = Forman
| first1 = J. R.
| title = Mechanical unfolding of proteins: Insights into biology, structure and folding
| journal = Current Opinion in Structural Biology
| volume = 17
| issue = 1
| pages = 58–66
| last2 = Clarke
| first2 = J
| doi = 10.1016/j.sbi.2007.01.006
}}</ref><ref>{{Cite journal
| pmid = 23265640
| pmc = 3578095
| year = 2013
| author1 = Nickson
| first1 = A. A.
| title = Take home lessons from studies of related proteins
| journal = Current Opinion in Structural Biology
| volume = 23
| issue = 1
| pages = 66–74
| last2 = Wensley
| first2 = B. G.
| last3 = Clarke
| first3 = J
| doi = 10.1016/j.sbi.2012.11.009
}}</ref><ref>{{Cite journal
| pmid = 22858055
| year = 2012
| author1 = Clarke
| first1 = J
| title = Learning from Nature to design new biomolecules
| journal = Current Opinion in Structural Biology
| volume = 22
| issue = 4
| pages = 395–6
| last2 = Schief
| first2 = W
| doi = 10.1016/j.sbi.2012.07.001
}}</ref><ref>{{Cite journal
| pmid = 20708403
| year = 2010
| author1 = Clarke
| first1 = J
| title = Protein engineering and design: From first principles to new technologies
| journal = Current Opinion in Structural Biology
| volume = 20
| issue = 4
| pages = 480–1
| last2 = Regan
| first2 = L
| doi = 10.1016/j.sbi.2010.07.001
}}</ref><ref>{{Cite journal
| pmid = 9519304
| year = 1998
| author1 = Clarke
| first1 = J
| title = Hydrogen exchange and protein folding
| journal = Current Opinion in Structural Biology
| volume = 8
| issue = 1
| pages = 112–8
| last2 = Itzhaki
| first2 = L. S.
| doi=10.1016/s0959-440x(98)80018-3
}}</ref> and the ''[[Journal of Molecular Biology]]''.<ref name=batey>{{Cite journal
| pmid = 18371978
| pmc = 2828540
| year = 2008
| author1 = Batey
| first1 = S
| title = The folding pathway of a single domain in a multidomain protein is not affected by its neighbouring domain
| journal = Journal of Molecular Biology
| volume = 378
| issue = 2
| pages = 297–301
| last2 = Clarke
| first2 = J
| doi = 10.1016/j.jmb.2008.02.032
}}</ref><ref name=batey2>{{Cite journal
| pmid = 15913648
| year = 2005
| author1 = Batey
| first1 = S
| title = Cooperative folding in a multi-domain protein
| journal = Journal of Molecular Biology
| volume = 349
| issue = 5
| pages = 1045–59
| last2 = Randles
| first2 = L. G.
| last3 = Steward
| first3 = A
| last4 = Clarke
| first4 = J
| doi = 10.1016/j.jmb.2005.04.028
}}</ref>
}}</ref>


==Awards and honours==
==Research and career==
Clarke was appointed a Wellcome Trust Senior Research Fellow in 2001, a Professor of Molecular Biophysics in 2009 and a Fellow of [[Trinity Hall, Cambridge]], in 2010.<ref name=whoswho/> On 1 October 2017, she became the [[Master (college)|President]] of [[Wolfson College, Cambridge]].<ref name="University of Cambridge"/>
In 2010, Clarke was awarded the US Genomics award from the [[Biophysical Society]].<ref>{{cite web|archiveurl=https://web.archive.org/web/20150408081944/http://www.biophysics.org/AwardsFunding/SocietyAwards/USGenomicsAward/tabid/505/Default.aspx|url=http://www.biophysics.org/AwardsFunding/SocietyAwards/USGenomicsAward/tabid/505/Default.aspx|title=US Genomics Award|publisher=Biophysical Society|archivedate=2015-04-08}}</ref> Clarke was also elected a [[Fellow of the Royal Society of Chemistry]] and a [[FMedSci|Fellow of the Academy of Medical Sciences (FMedSci)]] in 2013.<ref name=whoswho/> Her nomination for the [[Academy of Medical Sciences, United Kingdom|Academy of Medical Sciences]] reads: {{quote|Jane Clarke is a distinguished biophysical chemist at the University of Cambridge. She is recognised internationally for her multidisciplinary studies that have advanced the understanding of [[protein folding]] and misfolding. She pioneered the application of [[protein engineering]] techniques together with single molecule [[force spectroscopy]] and simulations to investigate the effect of force on proteins. For this she was awarded the [[Biophysical Society]] U.S Genomics Award for Outstanding Investigator in the field of [[Single-molecule experiment|Single Molecule Biology]] in 2010; at the time, the only non-US and still the only female recipient of this prestigious award.<ref name=fmedsci>{{cite web |author=Anon|year=2015|url=https://royalsociety.org |title = Professor Jane Clarke FMedSci |publisher=The Academy of Medical Sciences|archivedate=2015-04-08|archiveurl=https://web.archive.org/web/20150408081509/http://www.acmedsci.ac.uk/fellows/fellows-directory/ordinary-fellows/professor-jane-clarke/ |location=London}}</ref>}} Clarke was elected a [[List of Fellows of the Royal Society elected in 2015|Fellow of the Royal Society (FRS) in 2015]]. Her certificate of election reads: {{quote|Jane Clarke is distinguished for the rigorous physical chemistry approaches she has adapted and applied to understand protein folding and misfolding. Her fundamental studies revealed the presence of both parallel pathways and frustration in the [[energy landscape]] of apparently simple proteins. Most significantly, she has made very important advances in the study of multi-domain systems. From her discovery that aggregation and misfolding are determined by sequence similarity, through to her seminal studies combining force spectroscopy and protein engineering to elucidate mechanical unfolding energy landscapes, she has transformed our understanding of the evolution, folding and energetics of multidomain proteins.<ref name=royal>{{cite web|url=https://royalsociety.org/people/fellowship/2015/jane-clarke|archiveurl=https://web.archive.org/web/20150504202906/https://royalsociety.org/people/fellowship/2015/jane-clarke/|title=Professor Jane Clarke FMedSci FRS|publisher=Royal Society|location=London|archivedate=2015-05-04|author=Anon|year=2015}}</ref>}}

Clarke's research investigates [[protein folding]],<ref name=research>{{cite web|archive-url=https://web.archive.org/web/20130126033140/http://www-clarke.ch.cam.ac.uk/Research.php|url=http://www-clarke.ch.cam.ac.uk/Research.php|publisher=University of Cambridge|archive-date=2013-01-26|title=Jane Clarke Laboratory Research Areas}}</ref> in particular:
# Studies of [[Protein family|structurally related proteins]]
# [[Protein domain|Multidomain proteins]]: effects of sequence on folding and misfolding
# Folding and assembly: [[intrinsically disordered proteins]]

Clarke's research has been funded by the [[Wellcome Trust]],<ref name=wt>{{cite web|archive-url=https://web.archive.org/web/20140918043150/http://www.wellcome.ac.uk/Funding/Biomedical-science/Funded-projects/Awards-made/Wellcome-Fellows/WTD003235.htm|title=Senior Research Fellows in Basic Biomedical Science|publisher=Wellcome Trust|archive-date=2014-09-18|url=http://www.wellcome.ac.uk/Funding/Biomedical-science/Funded-projects/Awards-made/Wellcome-Fellows/WTD003235.htm}}</ref> [[Medical Research Council (United Kingdom)|Medical Research Council]] (MRC) and the [[Biotechnology and Biological Sciences Research Council]] (BBSRC).<ref name=gtr>{{cite web|archive-url=https://web.archive.org/web/20150413124239/http://gtr.rcuk.ac.uk/person/2F243482-207E-4F42-A2F5-77440C7E7154|title=UK Government Grants awarded Jane Clarke|publisher=[[Research Councils UK]]|url=http://gtr.rcuk.ac.uk/person/2F243482-207E-4F42-A2F5-77440C7E7154|archive-date=2015-04-13}}</ref>

She has been the author or co-author of over 100 scientific papers and book chapters<ref name=scopus /> including:
* Sigrid Milles and 11 other authors including Jane Clarke (2015) [https://www.cell.com/cell/pdf/S0092-8674(15)01264-7.pdf Plasticity of an ultrafast interaction between nucleoporins and nuclear transport receptors.] ''Cell'' '''163''' 734–745
* Madeleine B. Borgia, Alessandro Borgia, six others and Jane Clarke (2011) [http://europepmc.org/backend/ptpmcrender.fcgi?accid=PMC3160465&blobtype=pdf Single-molecule fluorescence reveals sequence-specific misfolding in multidomain proteins.] ''Nature'' '''474''' 662–665
* Alessandro Borgia, Philip M. Williams and Jane Clarke (2008) [https://www.annualreviews.org/doi/10.1146/annurev.biochem.77.060706.093102 Single-molecule studies of protein folding]. ''Annual Review of Biochemistry'' '''77''' 101–125
* Jung-Hoon Han, Sarah Batey, Adrian A. Nickson, Sarah A. Teichmann and Jane Clarke (2007) [https://www.nature.com/articles/nrm2144 The folding and evolution of multidomain proteins.] ''Nature Reviews Molecular Cell Biology'' '''8''' 319–330

===Awards and honours===
In 2010, Clarke was awarded the US [[Genomics]] award from the [[Biophysical Society]].<ref>{{cite web|archive-url=https://web.archive.org/web/20150408081944/http://www.biophysics.org/AwardsFunding/SocietyAwards/USGenomicsAward/tabid/505/Default.aspx|url=http://www.biophysics.org/AwardsFunding/SocietyAwards/USGenomicsAward/tabid/505/Default.aspx|title=US Genomics Award|publisher=Biophysical Society|archive-date=2015-04-08}}</ref> Clarke was also elected a [[Fellow of the Royal Society of Chemistry]] (FRSC){{when|date=December 2018}} and a [[Fellow of the Academy of Medical Sciences]] (FMedSci) in 2013.<ref name=whoswho/> Her nomination for the [[Academy of Medical Sciences, United Kingdom|Academy of Medical Sciences]] in 2013 reads: {{blockquote|Jane Clarke is a distinguished biophysical chemist at the University of Cambridge. She is recognised internationally for her multidisciplinary studies that have advanced the understanding of [[protein folding]] and misfolding. She pioneered the application of [[protein engineering]] techniques together with single molecule [[force spectroscopy]] and simulations to investigate the effect of force on proteins. For this she was awarded the [[Biophysical Society]] U.S Genomics Award for Outstanding Investigator in the field of [[Single-molecule experiment|Single Molecule Biology]] in 2010; at the time, the only non-US and still the only female recipient of this prestigious award.<ref name=fmedsci>{{cite web |author=Anon|year=2015|url=https://royalsociety.org |title = Professor Jane Clarke FMedSci |publisher=The Academy of Medical Sciences|archive-date=2015-04-08|archive-url=https://web.archive.org/web/20150408081509/http://www.acmedsci.ac.uk/fellows/fellows-directory/ordinary-fellows/professor-jane-clarke/ |location=London}}</ref>}} Clarke was elected a [[List of Fellows of the Royal Society elected in 2015|Fellow of the Royal Society (FRS) in 2015]]. Her certificate of election reads: {{blockquote|Jane Clarke is distinguished for the rigorous physical chemistry approaches she has adapted and applied to understand protein folding and misfolding. Her fundamental studies revealed the presence of both parallel pathways and frustration in the [[energy landscape]] of apparently simple proteins. Most significantly, she has made very important advances in the study of multi-domain systems. From her discovery that aggregation and misfolding are determined by sequence similarity, through to her seminal studies combining force spectroscopy and protein engineering to elucidate mechanical unfolding energy landscapes, she has transformed our understanding of the evolution, folding and energetics of multidomain proteins.<ref name=royal>{{cite web|url=https://royalsociety.org/people/fellowship/2015/jane-clarke|archive-url=https://web.archive.org/web/20150504202906/https://royalsociety.org/people/fellowship/2015/jane-clarke/|title=Professor Jane Clarke FMedSci FRS|publisher=Royal Society|location=London|archive-date=2015-05-04|author=Anon|year=2015}}</ref>}}


In 2021 she spoke about her career in the [[BBC Radio 4]] programme ''The Life Scientific''.<ref name="Clarke27 April 2021">{{cite web |title=Jane Clarke on Protein Folding|url=https://www.bbc.co.uk/programmes/m000vgh0|website=BBC }}</ref>
==Personal life==
Clarke married Christopher Clarke in 1973 and has one son and one daughter.<ref name=whoswho/>


==References==
==References==
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[[Category:Presidents of Wolfson College, Cambridge]]
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Latest revision as of 10:42, 30 September 2024

Jane Clarke
FRS FRSC FMedSci
Clarke in 2015
Born
Jane Morgan

(1950-09-10) 10 September 1950 (age 74)
London, England
Alma mater
Spouse
Christopher Clarke
​
(m. 1973)​
AwardsUS Genomics Award (2010)
Scientific career
Fields
Institutions
ThesisStudies of Disulphide Mutants of Barnase (1993)
Doctoral advisorAlan Fersht[1][2]
Websitewww-clarke.ch.cam.ac.uk

Jane Clarke (née Morgan; born 1950) is a British biochemist and academic. Since October 2017, she has served as President of Wolfson College, Cambridge.[4] She is also Professor of Molecular Biophysics, a Wellcome Trust Senior Research Fellow[5] in the Department of Chemistry at the University of Cambridge. She was previously a Fellow of Trinity Hall, Cambridge.[6][7][8] In 2023, she was elected to the National Academy of Sciences.[9]

Early life and education

[edit]

Clarke was born Jane Morgan in London on 10 September 1950. She was educated at the University of York where she graduated with a first-class honours degree in biochemistry in 1972.[3] She went on to study for a Postgraduate Certificate in Education (PGCE) at the University of Cambridge in 1973.[3] Clarke was a science teacher in several secondary schools, and a Head of Science at Northumberland Park School, Tottenham, from 1973 to 1986.[10]

Clarke married Christopher Clarke in 1973 with whom she would go on to have one son and one daughter.[3] He obtained a job in the United States and the family moved there. Since Clarke was unable to work as a teacher, through not having appropriate qualifications she decided to update her scientific knowledge through a Master of Science degree in applied biology, awarded in 1990 from the Georgia Institute of Technology. This experience made her decide to seek a career in research related to proteins.[10] She was subsequently awarded a Doctor of Philosophy degree in 1993 for investigations of Bacterial Ribonuclease (Barnase) from the University of Cambridge supervised by Alan Fersht.[1][2][11]

Research and career

[edit]

Clarke was appointed a Wellcome Trust Senior Research Fellow in 2001, a Professor of Molecular Biophysics in 2009 and a Fellow of Trinity Hall, Cambridge, in 2010.[3] On 1 October 2017, she became the President of Wolfson College, Cambridge.[4]

Clarke's research investigates protein folding,[12] in particular:

  1. Studies of structurally related proteins
  2. Multidomain proteins: effects of sequence on folding and misfolding
  3. Folding and assembly: intrinsically disordered proteins

Clarke's research has been funded by the Wellcome Trust,[5] Medical Research Council (MRC) and the Biotechnology and Biological Sciences Research Council (BBSRC).[13]

She has been the author or co-author of over 100 scientific papers and book chapters[7] including:

Awards and honours

[edit]

In 2010, Clarke was awarded the US Genomics award from the Biophysical Society.[14] Clarke was also elected a Fellow of the Royal Society of Chemistry (FRSC)[when?] and a Fellow of the Academy of Medical Sciences (FMedSci) in 2013.[3] Her nomination for the Academy of Medical Sciences in 2013 reads:

Jane Clarke is a distinguished biophysical chemist at the University of Cambridge. She is recognised internationally for her multidisciplinary studies that have advanced the understanding of protein folding and misfolding. She pioneered the application of protein engineering techniques together with single molecule force spectroscopy and simulations to investigate the effect of force on proteins. For this she was awarded the Biophysical Society U.S Genomics Award for Outstanding Investigator in the field of Single Molecule Biology in 2010; at the time, the only non-US and still the only female recipient of this prestigious award.[15]

Clarke was elected a Fellow of the Royal Society (FRS) in 2015. Her certificate of election reads:

Jane Clarke is distinguished for the rigorous physical chemistry approaches she has adapted and applied to understand protein folding and misfolding. Her fundamental studies revealed the presence of both parallel pathways and frustration in the energy landscape of apparently simple proteins. Most significantly, she has made very important advances in the study of multi-domain systems. From her discovery that aggregation and misfolding are determined by sequence similarity, through to her seminal studies combining force spectroscopy and protein engineering to elucidate mechanical unfolding energy landscapes, she has transformed our understanding of the evolution, folding and energetics of multidomain proteins.[16]

In 2021 she spoke about her career in the BBC Radio 4 programme The Life Scientific.[10]

References

[edit]
  1. ^ a b Anon (2015). "Women at Cambridge: Jane Clarke". University of Cambridge. Archived from the original on 24 March 2015.
  2. ^ a b Clarke, Jane (1993). Studies of disulphide mutants of barnase. jisc.ac.uk (PhD thesis). University of Cambridge. OCLC 53666398. EThOS uk.bl.ethos.318014. Archived from the original on 22 December 2018. Retrieved 22 December 2018.
  3. ^ a b c d e f Anon (2015). "Clarke, Prof. Jane". Who's Who (online Oxford University Press ed.). A & C Black. doi:10.1093/ww/9780199540884.013.U279617. (Subscription or UK public library membership required.)
  4. ^ a b "Introducing our new President: Professor Jane Clarke FMedSci FRS". Wolfson College. University of Cambridge. Retrieved 26 October 2017.[permanent dead link]
  5. ^ a b "Senior Research Fellows in Basic Biomedical Science". Wellcome Trust. Archived from the original on 18 September 2014.
  6. ^ "Professor Jane Clarke FMedSci, Biophysical and structural studies of protein folding". University of Cambridge. Archived from the original on 28 February 2014.
  7. ^ a b Jane Clarke publications indexed by the Scopus bibliographic database. (subscription required)
  8. ^ ORCID 0000-0002-7921-900X
  9. ^ "2023 NAS Election".
  10. ^ a b c "Jane Clarke on Protein Folding". BBC.
  11. ^ Clarke, J; Fersht, A. R. (1993). "Engineered disulfide bonds as probes of the folding pathway of barnase: Increasing the stability of proteins against the rate of denaturation". Biochemistry. 32 (16): 4322–9. doi:10.1021/bi00067a022. PMID 8476861.
  12. ^ "Jane Clarke Laboratory Research Areas". University of Cambridge. Archived from the original on 26 January 2013.
  13. ^ "UK Government Grants awarded Jane Clarke". Research Councils UK. Archived from the original on 13 April 2015.
  14. ^ "US Genomics Award". Biophysical Society. Archived from the original on 8 April 2015.
  15. ^ Anon (2015). "Professor Jane Clarke FMedSci". London: The Academy of Medical Sciences. Archived from the original on 8 April 2015.
  16. ^ Anon (2015). "Professor Jane Clarke FMedSci FRS". London: Royal Society. Archived from the original on 4 May 2015.
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