X-ray crystallographic studies of collagen-like peptides

Abstract

CRYSTALLOGRAPHY OF BIOLOGICAL MACROMOLECULES site is dictated by prefened geometry of the metal ion and not the structural constraints of the sunounding protein. This finding, which could not be adequately predicted by modeling studies done on this system, is key to the design of a metal binding site. Of the three metals, the binding of zinc results in the most favorable binding geometry, not dissimilar to those observed in naturally occurring zinc-binding proteins. This work represents the first successful X-ray crystallographic investigation of a de novo engineered metal binding site in the absence and presence of metal ions.

Effect of the Structural Water on the Mechanical Properties of Collagen-like Microfibrils: A Molecular Dynamics Study

“…Like collagen, the 1QSU molecule also has a triple-helical structure, its spatial assembly is quasihexagonal and staggered, and its structural water coordinates, known from crystallographical measurements, are also similar to that of collagen. 30 Unlike collagen type I, however, which is a heterotrimer (made of two a 1 chains and one a 2 chains), 1QSU is a homotrimer (made of three identical chains) and is relatively short (30 residues per chain, instead of 1,014 residues per chain in a native tropocollagen). Nevertheless, it is relatively slender (with an aspect ratio of around 7) and its intra-molecular and inter-molecular bonding patterns are analogous to that of true collagen.…”