Thermodynamics of helix-coil transitions studied by multicanonical algorithms
- Nara Women`s Univ. (Japan)
- Eidgenoessiche Technische Hochschule, Zuerich (Switzerland)
Thermodynamics of helix-coil transitions in amino acid homo-oligomers are studied by the recently proposed multicanonical algorithms. Homo-oligomers of length 10 are considered for three characteristic amino acids, alanine (helix former), valine (helix indifferent), and glycine (helix breaker). For alanine other lengths (15 and 20) are also considered in order to examine the length dependence. From one multicanonical production run with completely random initial conformations, we have obtained the lowest-energy conformations and various thermodynamic quantities (average helicity, Zimm-Bragg s and {sigma} parameters, free energy differences between helix and coil states, etc.) as functions of temperature. The results confirm the fact that alanine is helix-forming, valine is helix-indifferent, and glycine is helix-breaking. 36 refs., 10 figs., 5 tabs.
- Sponsoring Organization:
- USDOE
- OSTI ID:
- 92008
- Journal Information:
- Journal of Physical Chemistry, Vol. 99, Issue 28; Other Information: PBD: 13 Jul 1995
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
BASIC STUDIES
66 PHYSICS
99 MATHEMATICS
COMPUTERS
INFORMATION SCIENCE
MANAGEMENT
LAW
MISCELLANEOUS
ALANINES
THERMODYNAMICS
CONFORMATIONAL CHANGES
VALINE
GLYCINE
EXPERIMENTAL DATA
NUMERICAL DATA
AMINO ACIDS
ALGORITHMS
THERMODYNAMIC MOLECULAR MODEL
MOLECULAR STRUCTURE
SPECIFIC HEAT
PROBABILITY