Document Detail


High-pressure effect on the dynamics of solvated peptides.
MedLine Citation:
PMID:  22502549     Owner:  NLM     Status:  In-Data-Review    
Abstract/OtherAbstract:
The dynamics of peptides has a direct connection to how quickly proteins can alter their conformations. The speed of exploring the free energy landscape depend on many factors, including the physical parameters of the environment, such as pressure and temperature. We performed a series of molecular dynamics simulations to investigate the pressure-temperature effects on peptide dynamics, especially on the torsional angle and peptide-water hydrogen bonding (H-bonding) dynamics. Here, we show that the dynamics of the omega angle and the H-bonding dynamics between water and the peptide are affected by pressure. At high temperature (500 K), both the dynamics of the torsional angle ω and H-bonding slow down significantly with increasing pressure, interestingly, at approximately the same rate. However, at a lower temperature of 300 K, the observed trend on H-bonding dynamics as a function of pressure reverses, i.e., higher pressure speeds up H-bonding dynamics.
Authors:
Ricky B Nellas; Mary M Glover; Donald Hamelberg; Tongye Shen
Related Documents :
15080389 - Organizational instability and cardiovascular risk factors in white-collar employees: a...
15330389 - Cross-sectional study of cardiovascular effects of carbon disulfide among chinese worke...
10075379 - Microalbuminuria and hypertension in nondiabetic japanese men.
12118909 - Correlation between diastolic impairment and lipid metabolism in mild-to-moderate hyper...
2088799 - The antioxidant hypothesis of cardiovascular disease: epidemiology and mechanisms.
22412809 - Antihypertensive effect of long-term oral administration of jellyfish (rhopilema escule...
12057989 - Internal cardioversion of chronic atrial fibrillation during percutaneous mitral commis...
78849 - Postextrasystolic relaxation in the dog heart.
10728509 - Pitfalls in the diagnosis and management of systolic hypertension.
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  The Journal of chemical physics     Volume:  136     ISSN:  1089-7690     ISO Abbreviation:  J Chem Phys     Publication Date:  2012 Apr 
Date Detail:
Created Date:  2012-04-16     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0375360     Medline TA:  J Chem Phys     Country:  United States    
Other Details:
Languages:  eng     Pagination:  145103     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, Cellular & Molecular Biology, University of Tennessee, Knoxville, Tennessee 37996, USA.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:

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


Previous Document:  Tensegrity and motor-driven effective interactions in a model cytoskeleton.
Next Document:  Modified Wiener estimation of diffuse reflectance spectra from RGB values by the synthesis of new co...