Intermolecular interactions in type I collagens.
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.
David
C W
CW
Department of Chemistry, University of Connecticut, Storrs 06269-3060.
D000595:Amino Acid Sequence; D003094:Collagen / Q000737:chemistry* / Q000378:metabolism; D003198:Computer Simulation; D008969:Molecular Sequence Data
D003094:Collagen