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Molecular mechanics study of myelin basic protein
Author(s) -
Gilliom Richard D.,
Stoner Gerald L.
Publication year - 1987
Publication title -
journal of computational chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.907
H-Index - 188
eISSN - 1096-987X
pISSN - 0192-8651
DOI - 10.1002/jcc.540080806
Subject(s) - molecular mechanics , myelin , myelin basic protein , sequence (biology) , molecular dynamics , chemistry , myelin sheath , biophysics , physics , crystallography , computational chemistry , biology , biochemistry , central nervous system , neuroscience
Abstract Myelin basic protein (MBP) is the major extrinsic protein of the myelin sheath in the central nervous system. We have examined the predicted structure of segments of MBP using the molecular mechanics program ECEPP83 developed by Scheraga and coworkers as modified by Chuman, Momany, and Schafer. We have focused upon segments containing the Pro‐Pro‐Pro sequence (residues 100‐102), which have been predicted from standard algorithms to exist in a hairpin loop connecting anti‐parallel beta ‐strands. Both the shorter (98‐105, 99‐105, and 100‐105) and longer segments (87‐109, 87‐118, and 87‐120) have been examined. These results indicate potential for a chain reversal in this region. The shorter segments have been studied by others using NMR techniques and the results are compared.

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