Document Detail


Extensively hydrated but folded: a novel state of globular proteins stabilized at high pressure and low temperature.
MedLine Citation:
PMID:  22339877     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
We studied conformational fluctuations of the transcription factor c-Myb R2 subdomain (52 residues with three Trp) at high pressure and low temperature (5°C) using two different spectroscopic methods, Trp fluorescence and (1)H NMR, on its chemically stable mutant C130I (pseudo-wild-type (WT(S))), which has a large internal cavity. As pressure was increased from 3 to 300 MPa, the Trp fluorescence λ(max) of WT(S) shifted from 342 to ∼355 nm, clearly showing that the three Trp rings become fully exposed to the polar environment, which usually is taken to indicate that the protein underwent unfolding. In contrast, as pressure was increased from 3 to 300 MPa, the high-field-shifted (1)H NMR signals characteristic of the folded state showed a still higher-field shift, but no significant changes in their intensity. The last result unequivocally shows that the protein remains largely folded at 300 MPa. The apparent discrepancy between the two predictions would only be solved if one were to postulate the existence of an extensively hydrated but folded state in WT(S). Intriguingly, such a state was not found in a cavity-filling mutant of WT(S), C130I/V103L, suggesting that this state is mediated by cavity hydration. The generality and significance of this state in proteins are discussed.
Authors:
Sunilkumar Puthenpurackal Narayanan; Akihiro Maeno; Hiroshi Matsuo; Masayuki Oda; Hisayuki Morii; Kazuyuki Akasaka
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biophysical journal     Volume:  102     ISSN:  1542-0086     ISO Abbreviation:  Biophys. J.     Publication Date:  2012 Jan 
Date Detail:
Created Date:  2012-02-20     Completed Date:  2012-06-07     Revised Date:  2013-06-26    
Medline Journal Info:
Nlm Unique ID:  0370626     Medline TA:  Biophys J     Country:  United States    
Other Details:
Languages:  eng     Pagination:  L8-10     Citation Subset:  IM    
Copyright Information:
Copyright © 2012 Biophysical Society. Published by Elsevier Inc. All rights reserved.
Affiliation:
Graduate School of Biology-Oriented Science and Technology, Kinki University, Kinokawa, Japan.
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MeSH Terms
Descriptor/Qualifier:
Models, Molecular
Mutation
Pressure*
Protein Folding*
Protein Stability
Protein Structure, Tertiary
Proto-Oncogene Proteins c-myb / chemistry*,  genetics
Temperature*
Water / chemistry*
Chemical
Reg. No./Substance:
0/Proto-Oncogene Proteins c-myb; 7732-18-5/Water
Comments/Corrections

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