Liu, F and Du, D and Fuller, AA and Davoren, JE and Wipf, P and Kelly, JW and Gruebele, M
(2008)
An experimental survey of the transition between two-state and downhill protein folding scenarios.
Proceedings of the National Academy of Sciences of the United States of America, 105 (7).
2369 - 2374.
ISSN 0027-8424
Abstract
A kinetic and thermodynamic survey of 35 WW domain sequences is used in combination with a model to discern the energetic requirements for the transition from two-state folding to downhill folding. The sequences used exhibit a 600-fold range of folding rates at the temperature of maximum folding rate. Very stable proteins can achieve complete downhill folding when the temperature is lowered sufficiently below the melting temperature, and then at even lower temperatures they become two-state folders again because of cold denaturation. Less stable proteins never achieve a sufficient bias to fold downhill because of the onset of cold denaturation. The model, considering both heat and cold denaturation, reveals that to achieve incipient downhill folding (barrier <3 RT) or downhill folding (no barrier), the WW domain average melting temperatures have to be >50°C for incipient downhill folding and >90°C for downhill folding. © 2008 by The National Academy of Sciences of the USA.
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Item Type: |
Article
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Status: |
Published |
Creators/Authors: |
Creators | Email | Pitt Username | ORCID ![](/images/orcid_id_24x24.png) |
---|
Liu, F | | | | Du, D | | | | Fuller, AA | | | | Davoren, JE | | | | Wipf, P | pwipf@pitt.edu | PWIPF | | Kelly, JW | | | | Gruebele, M | | | |
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Date: |
19 February 2008 |
Date Type: |
Publication |
Journal or Publication Title: |
Proceedings of the National Academy of Sciences of the United States of America |
Volume: |
105 |
Number: |
7 |
Page Range: |
2369 - 2374 |
DOI or Unique Handle: |
10.1073/pnas.0711908105 |
Schools and Programs: |
Dietrich School of Arts and Sciences > Chemistry |
Refereed: |
Yes |
ISSN: |
0027-8424 |
MeSH Headings: |
Amino Acid Sequence; Humans; Kinetics; Models, Molecular; Molecular Sequence Data; Protein Denaturation; Protein Folding; Protein Structure, Tertiary; Proteins; Temperature; Thermodynamics |
Other ID: |
NLM PMC2268143 |
PubMed Central ID: |
PMC2268143 |
PubMed ID: |
18268349 |
Date Deposited: |
22 Jul 2013 18:21 |
Last Modified: |
26 Sep 2022 16:51 |
URI: |
http://d-scholarship.pitt.edu/id/eprint/19346 |
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