New theoretical methodology for elucidating the solution structure of peptides from NMR data. 1. The relative contribution of low-energy microstates to the partition function

Journal Article · Thu Mar 30 04:00:00 EST 1995 · Journal of Physical Chemistry

DOI:https://doi.org/10.1021/j100013a065· OSTI ID:83130

Meirovitch, H; Meirovitch, E; Lee, J ^[1]

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1. Florida State Univ., Tallahassee, FL (United States)

A new theoretical methodology is developed for treating ensembles of interconverting conformations which is based on purely thermodynamic grounds. The peptide is described by a potential energy function, and its conformational space is viewed as a collection of microstates, which are local conformational regions around energy minima. The overall methodology enables one to identify the thermodynamically most stable microstates, determine their populations, calculate the individual microstate nuclear Overhauser enhancement spectra (NOEs) and obtain the overall NOEs as averages over the individual contributions, weighted by the microstate populations. This paper develops theoretical methods for calculating the relative contribution of microstates to the partition function, as their minimum energy is increased above the global energy minimum. 47 refs., 1 fig., 4 tabs.

• Sponsoring Organization: USDOE
• OSTI ID: 83130
• Journal Information: Journal of Physical Chemistry, Journal Name: Journal of Physical Chemistry Journal Issue: 13 Vol. 99; ISSN JPCHAX; ISSN 0022-3654
• Country of Publication: United States
• Language: English

Related Subjects

40 CHEMISTRY
66 PHYSICS
ENTROPY
NUCLEAR MAGNETIC RESONANCE
NUMERICAL DATA
PARTITION FUNCTIONS
PEPTIDES
POTENTIALS
PROBABILITY
SPECTROSCOPY
THERMODYNAMIC PROPERTIES