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Intermolecular interactions in type I collagens
Author(s) -
David Carl W.
Publication year - 1992
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.300050303
Subject(s) - intermolecular force , chemistry , fibril , molecule , chain (unit) , intermolecular interaction , biophysics , offset (computer science) , crystallography , stereochemistry , biochemistry , organic chemistry , physics , computer science , biology , astronomy , programming language
Abstract X‐PLOR modelling of collagen dimers containing Gly‐Glu‐Arg in each chain has been carried out. The interaction between molecules when two Gly_Glu‐Arg are present on each chain is found to be substantially less than two times that obtained with one per chain, implying that relative tilting of two collagen molecules does not offset the disadvantages of misalignment of the interacting moieties. This implies that if multiple (Glu − ‐Arg + ) 3 interactions are important in fibril formation, their lateral separations must be large enough to insure that they act independently.