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An experimental survey of the transition between two-state and downhill protein folding scenarios

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

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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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Details

Item Type: Article
Status: Published
Creators/Authors:
CreatorsEmailPitt UsernameORCID
Liu, F
Du, D
Fuller, AA
Davoren, JE
Wipf, Ppwipf@pitt.eduPWIPF
Kelly, JW
Gruebele, M
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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