title: Fibrous Protein Structures: Hierarchy, History and Heroes.
abstract: During the 1930s and 1940s the technique of X-ray diffraction was applied widely by William Astbury and his colleagues to a number of naturally-occurring fibrous materials. On the basis of the diffraction patterns obtained, he observed that the structure of each of the fibres was dominated by one of a small number of different types of molecular conformation. One group of fibres, known as the k-m-e-f group of proteins (keratin - myosin - epidermin - fibrinogen), gave rise to diffraction characteristics that became known as the α-pattern. Others, such as those from a number of silks, gave rise to a different pattern - the β-pattern, while connective tissues yielded a third unique set of diffraction characteristics. At the time of Astbury's work, the structures of these materials were unknown, though the spacings of the main X-ray reflections gave an idea of the axial repeats and the lateral packing distances. In a breakthrough in the early 1950s, the basic structures of all of these fibrous proteins were determined. It was found that the long protein chains, composed of strings of amino acids, could be folded up in a systematic manner to generate a limited number of structures that were consistent with the X-ray data. The most important of these were known as the α-helix, the β-sheet, and the collagen triple helix. These studies provided information about the basic building blocks of all proteins, both fibrous and globular. They did not, however, provide detailed information about how these molecules packed together in three-dimensions to generate the fibres found in vivo. A number of possible packing arrangements were subsequently deduced from the X-ray diffraction and other data, but it is only in the last few years, through the continued improvements of electron microscopy, that the packing details within some fibrous proteins can now be seen directly. Here we outline briefly some of the milestones in fibrous protein structure determination, the role of the amino acid sequences and how new techniques, including electron microscopy, are helping to define fibrous protein structures in three-dimensions. We also introduce the idea that, from the known sequence characteristics of different fibrous proteins, new molecules can be designed and synthesized, thereby generating new biological materials with specific structural properties. Some of these, for example, are planned for use in drug delivery systems. Along the way we also introduce the various Chapters of the book, where individual fibrous proteins are discussed in detail.
authors.affiliation: Muscle Contraction Group, School of Physiology, Pharmacology and Neuroscience, University of Bristol, Bristol, BS8 1TD, UK. j.squire@imperial.ac.uk.
authors.forename: John M
authors.initials: JM
authors.lastname: Squire
authors.affiliation: Institute of Fundamental Sciences and Riddet Institute, Massey University, Private Bag 11-222, Palmerston North, 4442, New Zealand.
authors.forename: David A D
authors.initials: DA
authors.lastname: Parry
mesh_terms: D000596:Amino Acids / Q000737:chemistry; D000818:Animals; D018360:Crystallography, X-Ray / Q000266:history / Q000379:methods; D049673:History, 20th Century; D049674:History, 21st Century; D006801:Humans; D008958:Models, Molecular; D017433:Protein Structure, Secondary; D012596:Scleroproteins / Q000737:chemistry*
chemical_list: D000596:Amino Acids; D012596:Scleroproteins
keywords: Amino acid sequence; Coiled-coil; Collagen fold; Cross-β structure; Heptad; Stammers; Stutters; α-helix; β-pleated sheet