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- W123937820 abstract "X-Ray structure determinations have been made of several partially crystalline polypeptide-solvent systems. By comparing these structures with those of the dry polypeptides, an investigation has been made of the effects of solvent incorporation on the conformation and packing of the polypeptide chains. Polyproline I forms two complexes with propionic acid. In one case there are alternating sheets of polypeptide and solvent, in the other the chains pack tetragonally and enclose columns of solvent. In both complexes there are van der Waals contacts between polypeptide chains and these have the same conformation as in the dry hexagonally packed form. In two systems involving polytripeptides related to collagen, (Pro-Gly-Gly)n—formic acid and (Pro-Gly-Pro)n—water, solvent incorporation does not affect either polypeptide conformation or interchain hydrogen bonding. Poly-γ-benzyl-L-glutamate in a cholesteric phase with m-cresol has an α-helical conformation, as in the dry form. Polylysine hydrochloride undergoes a series of reversible packing and conformational changes with increasing hydration. Its structure which is of the β-pleated sheet type at low relative humidity, changes to α-helical at 84% r.h. and to random coil in dilute solution. Polyarginine hydrochloride shows similar structural changes with variations in hydration. In this case, however, the dry form is α-helical and a transition to a β conformation occurs at water contents exceeding five molecules per arginine residue. Apart from a few major conformational changes with fairly sharp transitions, the polypeptides studied show an invariability of conformation over a wide range of solvation and intermolecular distance." @default.
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- W123937820 date "1967-01-01" @default.
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- W123937820 title "Some X-Ray Studies Concerning the Influence of Solvents on Polypeptide Structures" @default.
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- W123937820 doi "https://doi.org/10.1016/b978-1-4832-2843-3.50005-4" @default.
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