Electronic Resource
College Park, Md.
:
American Institute of Physics (AIP)
The Journal of Chemical Physics
102 (1995), S. 3396-3403
ISSN:
1089-7690
Source:
AIP Digital Archive
Topics:
Physics
,
Chemistry and Pharmacology
Notes:
Theoretical methods are developed and applied to the protein crambin as a model system to characterize collective normal mode dynamics and their effects on correlations between torsion angle fluctuations and heteronuclear NMR relaxation parameters. Backbone N–H NMR S2 order parameters are found to be predominantly determined by local cursive-phi and ψ torsion angle fluctuations induced by collective protein modes. The ratio between Cβ–Hβ and Cα–Hα order parameters directly yields fluctuation amplitudes of the sidechain χ1 torsion angles. The results allow a more direct interpretation of motional effects monitored by nuclear spin relaxation. © 1995 American Institute of Physics.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1063/1.469213
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