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.uri |
https://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.language |
eng |
|
dc.language.iso |
en_US |
|
dc.publisher |
American Chemical Society (ACS) |
|
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 |
|
|
dc.type |
Journal article |
|
duke.contributor.id |
Lin, SS|0088645 |
|
duke.contributor.id |
Bowles, DE|0334339 |
|
duke.contributor.id |
Parker, W|0115196 |
|
dc.description.version |
Version of Record |
|
duke.date.pubdate |
2010-7-6 |
|
duke.description.issue |
26 |
|
duke.description.volume |
49 |
|
dc.relation.journal |
Biochemistry |
|
pubs.author-url |
http://www.ncbi.nlm.nih.gov/pubmed/20515035 |
|
pubs.begin-page |
5609 |
|
pubs.end-page |
5619 |
|
pubs.issue |
26 |
|
pubs.organisational-group |
Basic Science Departments |
|
pubs.organisational-group |
Clinical Science Departments |
|
pubs.organisational-group |
Duke |
|
pubs.organisational-group |
Immunology |
|
pubs.organisational-group |
Pathology |
|
pubs.organisational-group |
School of Medicine |
|
pubs.organisational-group |
Surgery |
|
pubs.organisational-group |
Surgery, Cardiovascular and Thoracic Surgery |
|
pubs.organisational-group |
Surgery, Surgical Sciences |
|
pubs.publication-status |
Published |
|
pubs.volume |
49 |
|
dc.identifier.eissn |
1520-4995 |
|
duke.contributor.orcid |
Parker, W|0000-0003-3644-9152 |
|