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dc.contributor.author Chen, E
dc.contributor.author Everett, ML
dc.contributor.author Holzknecht, ZE
dc.contributor.author Holzknecht, RA
dc.contributor.author Lin, SS
dc.contributor.author Bowles, DE
dc.contributor.author Parker, W
dc.coverage.spatial United States
dc.date.accessioned 2011-06-21T17:22:09Z
dc.date.issued 2010-07-06
dc.identifier http://www.ncbi.nlm.nih.gov/pubmed/20515035
dc.identifier.citation Biochemistry, 2010, 49 (26), pp. 5609 - 5619
dc.identifier.uri http://hdl.handle.net/10161/4008
dc.description.abstract Several lines of evidence point strongly toward the importance of highly alpha-helical intermediates in the folding of all globular proteins, regardless of their native structure. However, experimental refolding studies demonstrate no observable alpha-helical intermediate during refolding of some beta-sheet proteins and have dampened enthusiasm for this model of protein folding. In this study, beta-sheet proteins were hypothesized to have potential to form amphiphilic helices at a period of <3.6 residues/turn that matches or exceeds the potential at 3.6 residues/turn. Hypothetically, such potential is the basis for an effective and unidirectional mechanism by which highly alpha-helical intermediates might be rapidly disassembled during folding and potentially accounts for the difficulty in detecting highly alpha-helical intermediates during the folding of some proteins. The presence of this potential was confirmed, indicating that a model entailing ubiquitous formation of alpha-helical intermediates during the folding of globular proteins predicts previously unrecognized features of primary structure. Further, the folding of fatty acid binding protein, a predominantly beta-sheet protein that exhibits no apparent highly alpha-helical intermediate during folding, was dramatically accelerated by 2,2,2-trifluoroethanol, a solvent that stabilizes alpha-helical structure. This observation suggests that formation of an alpha-helix can be a rate-limiting step during folding of a predominantly beta-sheet protein and further supports the role of highly alpha-helical intermediates in the folding of all globular proteins.
dc.format.extent 5609 - 5619
dc.language ENG
dc.language.iso en_US en_US
dc.relation.ispartof Biochemistry
dc.relation.isversionof 10.1021/bi100288q
dc.subject Fatty Acid-Binding Proteins
dc.subject Kinetics
dc.subject Models, Molecular
dc.subject Protein Folding
dc.subject Protein Structure, Secondary
dc.subject Solvents
dc.title Short-lived alpha-helical intermediates in the folding of beta-sheet proteins.
dc.title.alternative en_US
dc.type Journal Article
dc.description.version Version of Record en_US
duke.date.pubdate 2010-7-6 en_US
duke.description.endpage 5619 en_US
duke.description.issue 26 en_US
duke.description.startpage 5609 en_US
duke.description.volume 49 en_US
dc.relation.journal Biochemistry en_US
pubs.author-url http://www.ncbi.nlm.nih.gov/pubmed/20515035
pubs.issue 26
pubs.organisational-group /Duke
pubs.organisational-group /Duke/School of Medicine
pubs.organisational-group /Duke/School of Medicine/Basic Science Departments
pubs.organisational-group /Duke/School of Medicine/Basic Science Departments/Immunology
pubs.organisational-group /Duke/School of Medicine/Clinical Science Departments
pubs.organisational-group /Duke/School of Medicine/Clinical Science Departments/Pathology
pubs.organisational-group /Duke/School of Medicine/Clinical Science Departments/Surgery
pubs.organisational-group /Duke/School of Medicine/Clinical Science Departments/Surgery/Surgery, Cardiovascular and Thoracic Surgery
pubs.organisational-group /Duke/School of Medicine/Clinical Science Departments/Surgery/Surgery, Surgical Sciences
pubs.publication-status Published
pubs.volume 49
dc.identifier.eissn 1520-4995

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