Document Detail

Cooperative cold denaturation: the case of the C-terminal domain of ribosomal protein L9.
MedLine Citation:
PMID:  23461364     Owner:  NLM     Status:  MEDLINE    
Cold denaturation is a general property of globular proteins, but it is difficult to directly characterize because the transition temperature of protein cold denaturation, T(c), is often below the freezing point of water. As a result, studies of protein cold denaturation are often facilitated by addition of denaturants, using destabilizing pHs or extremes of pressure, or reverse micelle encapsulation, and there are few studies of cold-induced unfolding under near native conditions. The thermal and denaturant-induced unfolding of single-domain proteins is usually cooperative, but the cooperativity of cold denaturation is controversial. The issue is of both fundamental and practical importance because cold unfolding may reveal information about otherwise inaccessible partially unfolded states and because many therapeutic proteins need to be stabilized against cold unfolding. It is thus desirable to obtain more information about the process under nonperturbing conditions. The ability to access cold denaturation in native buffer is also very useful for characterizing protein thermodynamics, especially when other methods are not applicable. In this work, we study a point mutant of the C-terminal domain of ribosomal protein L9 (CTL9), which has a T(c) above 0 °C. The mutant was designed to allow the study of cold denaturation under near native conditions. The cold denaturation process of I98A CTL9 was characterized by nuclear magnetic resonance, circular dichroism, and Fourier transform infrared spectroscopy. The results are consistent with apparently cooperative, two-state cold unfolding. Small-angle X-ray scattering studies show that the unfolded state expands as the temperature is lowered.
Bowu Luan; Bing Shan; Carlos Baiz; Andrei Tokmakoff; Daniel P Raleigh
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2013-03-26
Journal Detail:
Title:  Biochemistry     Volume:  52     ISSN:  1520-4995     ISO Abbreviation:  Biochemistry     Publication Date:  2013 Apr 
Date Detail:
Created Date:  2013-04-09     Completed Date:  2013-05-29     Revised Date:  2014-04-08    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  United States    
Other Details:
Languages:  eng     Pagination:  2402-9     Citation Subset:  IM    
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MeSH Terms
Bacterial Proteins / chemistry*,  genetics
Circular Dichroism
Cold Temperature
Geobacillus stearothermophilus / chemistry*,  genetics
Models, Molecular
Nuclear Magnetic Resonance, Biomolecular
Point Mutation
Protein Denaturation*
Protein Structure, Tertiary
Ribosomal Proteins / chemistry*,  genetics
Scattering, Small Angle
Spectroscopy, Fourier Transform Infrared
X-Ray Diffraction
Reg. No./Substance:
0/Bacterial Proteins; 0/Ribosomal Proteins; 0/ribosomal protein L9

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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