Title
Inclusion of solvation free energy with molecular mechanics energy: alanyl dipeptide as a test case
UMMS Affiliation
Department of Biochemistry and Molecular Pharmacology
Publication Date
1992-03-01
Document Type
Article
Subjects
Calorimetry; Dipeptides; Models, Chemical; *Protein Conformation; Quantum Theory; Thermodynamics
Disciplines
Biochemistry, Biophysics, and Structural Biology | Pharmacology, Toxicology and Environmental Health
Abstract
A combined force field of molecular mechanics and solvation free energy is tested by carrying out energy minimization and molecular dynamics on several conformations of the alanyl dipeptide. Our results are qualitatively consistent with previous experimental and computational studies, in that the addition of solvation energy stabilizes the C5 conformation of the alanyl dipeptide relative to the C7.
Keywords
alanyl dipeptide, energy minimization, molecular dynamics, molecular mechanics, solvation free energy
DOI of Published Version
10.1002/pro.5560010311
Source
Protein Sci. 1992 Mar;1(3):396-400. Link to article on publisher's site
Journal/Book/Conference Title
Protein science : a publication of the Protein Society
Related Resources
PubMed ID
1304346
Repository Citation
Schiffer CA, Caldwell JW, Stroud RM, Kollman PA. (1992). Inclusion of solvation free energy with molecular mechanics energy: alanyl dipeptide as a test case. Biochemistry and Molecular Pharmacology Publications. https://doi.org/10.1002/pro.5560010311. Retrieved from https://escholarship.umassmed.edu/bmp_pp/103