title: Fifty years of fibrous protein research: a personal retrospective.
abstract: As a result of X-ray fiber diffraction studies on fibrous proteins and crystallographic data on fragments derived from them, new experimental techniques across the biophysical and biochemical spectra, sophisticated computer modeling and refinement procedures, widespread use of bioinformatics and improved specimen preparative procedures the structures of many fibrous proteins have now been determined to at least low resolution. In so doing these structures have yielded insight into the relationship that exists between sequence and conformation and this, in turn, has led to improved methodologies for predicting structure from sequence data alone. In this personal retrospective a selection of progress made during the past 50years is discussed in terms of events to which the author has made some contribution.
authors.affiliation: Institute of Fundamental Sciences, Massey University, Private Bag 11-222, Palmerston North 4442, New Zealand. Electronic address: d.parry@massey.ac.nz.
authors.forename: David A D
authors.initials: DA
authors.lastname: Parry
mesh_terms: D035843:Biomedical Research / Q000266:history*; D001703:Biophysics / Q000379:methods; D018360:Crystallography, X-Ray; D049673:History, 20th Century; D007633:Keratins / Q000737:chemistry; D008958:Models, Molecular; D051179:Plakins / Q000737:chemistry; D011487:Protein Conformation; D012596:Scleroproteins / Q000737:chemistry*; D014335:Tropomyosin / Q000737:chemistry; D014961:X-Ray Diffraction
chemical_list: D051179:Plakins; D012596:Scleroproteins; D014335:Tropomyosin; D007633:Keratins
keywords: Coiled-coil proteins; Collagen; Connective tissue; Heptads; Muscle; Plakins; Synthetic polypeptides; Tropomyosin; α-, β- and feather keratin