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International
Tables for Crystallography Volume F Crystallography of biological macromolecules Edited by M. G. Rossmann and E. Arnold © International Union of Crystallography 2006 |
International Tables for Crystallography (2006). Vol. F. ch. 19.5, p. 449
Section 19.5.8.1. Polypeptides
aWhistler Center for Carbohydrate Research, Purdue University, West Lafayette, IN 47907, USA, and bDepartment of Molecular Biology, Vanderbilt University, Nashville, TN 37235, USA |
The structural details of the α-helix and β-sheet, the principal secondary-structure elements of proteins, have emerged from the analysis of synthetic polypeptides (Pauling & Corey, 1951![[link]](/graphics/greenarr.gif)
, 1953). Analysis of noncrystalline fibre-diffraction patterns led to the triple-helical coiled-coil model of collagen (Ramachandran & Kartha, 1955; Rich & Crick, 1955). Recent studies on the organization of β-sheets in peptides of up to about 45 residues are providing an understanding of the molecular details of amyloid fibrils, related to Alzheimer's disease (Inouye et al., 1993; Malinchik et al., 1998).
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