Document Detail

Protein elasticity determined by pressure tuning of the tyrosine residue of ubiquitin.
MedLine Citation:
PMID:  17824766     Owner:  NLM     Status:  MEDLINE    
We determined the isotropic, isothermal compressibility of ubiquitin by pressure tuning spectral holes burnt into the red edge of the absorption spectrum of the single tyrosine residue. The pressure shift is perfectly linear with burn frequency. From these data, a compressibility of 0.086 GPa(-1) in the local environment of the tyrosine residue could be determined. This value fits nicely into the range known for proteins. Although the elastic behavior at low temperatures does not show any unusual features, the pressure tuning behavior at room temperature is quite surprising: the pressure-induced spectral shift is close to zero, even up to very high pressure levels of 0.88 GPa, well beyond the denaturation point. The reason for this behavior is attributed to equally strong blue as well as red spectral pressure shifts resulting in an average pressure-induced solvent shift that is close to zero.
Mark M Somoza; Johannes Wiedersich; Josef Friedrich
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Journal of chemical physics     Volume:  127     ISSN:  0021-9606     ISO Abbreviation:  J Chem Phys     Publication Date:  2007 Sep 
Date Detail:
Created Date:  2007-09-10     Completed Date:  2007-11-13     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0375360     Medline TA:  J Chem Phys     Country:  United States    
Other Details:
Languages:  eng     Pagination:  095102     Citation Subset:  IM    
Physik-Department E14 and Lehrstuhl für Physik Weihenstephan, Technische Universität München, 85350 Freising, Germany.
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MeSH Terms
Computer Simulation
Models, Chemical*
Models, Molecular*
Protein Conformation
Stress, Mechanical
Tyrosine / chemistry*
Ubiquitin / chemistry*,  ultrastructure*
Reg. No./Substance:
0/Ubiquitin; 55520-40-6/Tyrosine

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

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