Publication Date:
1987-05-01
Description:
A fundamental problem in chemistry and biochemistry is understanding the role of solvation in determining molecular properties. Recent advances in statistical mechanical theory and molecular dynamics methodology can be used to solve this problem with the aid of supercomputers. By using these advances the free energies of solvation of all the chemical classes of amino acid side chains, four nucleic acid bases and other organic molecules can be calculated. The effect of a site-specific mutation on the stability of trypsin is predicted. The results are in good agreement with available experiments.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bash, P A -- Singh, U C -- Langridge, R -- Kollman, P A -- CA-25644/CA/NCI NIH HHS/ -- GM-29072/GM/NIGMS NIH HHS/ -- RR-1081/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1987 May 1;236(4801):564-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3576184" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acids
;
Chemistry, Physical
;
*Computer Simulation
;
Hydrogen Bonding
;
Models, Chemical
;
Mutation
;
Physicochemical Phenomena
;
Purines
;
Pyrimidines
;
Solvents
;
*Thermodynamics
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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