eprintid: 19346
rev_number: 18
userid: 1419
dir: disk0/00/01/93/46
datestamp: 2013-07-22 18:21:42
lastmod: 2019-02-02 15:57:10
status_changed: 2013-07-22 18:21:42
type: article
metadata_visibility: show
item_issues_count: 0
eprint_status: archive
creators_name: Liu, F
creators_name: Du, D
creators_name: Fuller, AA
creators_name: Davoren, JE
creators_name: Wipf, P
creators_name: Kelly, JW
creators_name: Gruebele, M
creators_email: 
creators_email: 
creators_email: 
creators_email: 
creators_email: pwipf@pitt.edu
creators_email: 
creators_email: 
creators_id: 
creators_id: 
creators_id: 
creators_id: 
creators_id: PWIPF
creators_id: 
creators_id: 
title: An experimental survey of the transition between two-state and downhill protein folding scenarios
ispublished: pub
divisions: sch_as_chemistry
full_text_status: public
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.
date: 2008-02-19
date_type: published
publication: Proceedings of the National Academy of Sciences of the United States of America
volume: 105
number: 7
pagerange: 2369 - 2374
refereed: TRUE
issn: 0027-8424
id_number: 10.1073/pnas.0711908105
other_id: NLM PMC2268143
pmcid: PMC2268143
pmid: 18268349
mesh_headings: Amino Acid Sequence
mesh_headings: Humans
mesh_headings: Kinetics
mesh_headings: Models, Molecular
mesh_headings: Molecular Sequence Data
mesh_headings: Protein Denaturation
mesh_headings: Protein Folding
mesh_headings: Protein Structure, Tertiary
mesh_headings: Proteins
mesh_headings: Temperature
mesh_headings: Thermodynamics
chemical_names: Proteins
citation:   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     
document_url: http://d-scholarship-dev.library.pitt.edu/19346/1/licence.txt