Document Detail

Low-temperature studies of encapsulated proteins.
MedLine Citation:
PMID:  16190719     Owner:  NLM     Status:  MEDLINE    
Water-soluble proteins encapsulated within reverse micelles may be studied under a variety of conditions, including low temperature and a wide range of buffer conditions. Direct high-resolution detection of information relating to protein folding intermediates and pathways can be monitored by low-temperature solution NMR. Ubiquitin encapsulated within AOT reverse micelles was studied using multidimensional multinuclear solution NMR to determine the relationship between protein structure, temperature, and ionic strength. Ubiquitin resonances were monitored by 15N HSQC NMR experiments at varying temperatures and salt concentrations. Our results indicate that the structure of the encapsulated protein at low temperature experiences perturbation arising from two major influences, which are reverse micelle-protein interactions and low-temperature effects (e.g., cold denaturation). These two effects are impossible to distinguish under conditions of low ionic strength. Elevated concentrations of nondenaturing salt solutions defeat the effects of reverse micelle-protein interactions and reveal low-temperature protein unfolding. High ionic strength shielding stabilizes the reverse micelle at low temperatures, which reduces the electrostatic interaction between the protein and reverse micelle surfaces, allowing the phenomenon of cold denaturation to be explored.
Wade D Van Horn; Alana K Simorellis; Peter F Flynn
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Journal of the American Chemical Society     Volume:  127     ISSN:  0002-7863     ISO Abbreviation:  J. Am. Chem. Soc.     Publication Date:  2005 Oct 
Date Detail:
Created Date:  2005-09-29     Completed Date:  2006-01-23     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  7503056     Medline TA:  J Am Chem Soc     Country:  United States    
Other Details:
Languages:  eng     Pagination:  13553-60     Citation Subset:  IM    
Department of Chemistry, University of Utah, Salt Lake City, Utah 84112-0850, USA.
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MeSH Terms
Cold Temperature*
Nuclear Magnetic Resonance, Biomolecular
Osmolar Concentration
Protein Denaturation
Proteins / chemistry*
Grant Support
Reg. No./Substance:
0/Micelles; 0/Proteins

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

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