Kenneth Bailey

Research Article| January 01 1948 Tropomyosin: a new asymmetric protein component of the muscle fibril K. Bailey K. Bailey 1Biochemical Laboratory, University of Cambridge Search for other works by this author on: This Site PubMed Google Scholar Biochem J (1948) 43 (2): 271–279. https://doi.org/10.1042/bj0430271 Views Icon Views Article contents Figures & tables Video Audio Supplementary Data Peer Review Share Icon Share Facebook Twitter LinkedIn MailTo Cite Icon Cite Get Permissions Citation K. Bailey; Tropomyosin: a new asymmetric protein component of the muscle fibril. Biochem J 1 January 1948; 43 (2): 271–279. doi: https://doi.org/10.1042/bj0430271 Download citation file: Ris (Zotero) Reference Manager EasyBib Bookends Mendeley Papers EndNote RefWorks BibTex toolbar search Search Dropdown Menu toolbar search search input Search input auto suggest filter your search All ContentAll JournalsBiochemical Journal Search Advanced Search This content is only available as a PDF. © 1948 CAMBRIDGE UNIVERSITY PRESS1948 Article PDF first page preview Close Modal You do not currently have access to this content.

THE X-ray diffraction photographs usually obtained from apparently nonfibrous proteins have so much in common with one another and with the photographs given by certain natural protein fibres when disoriented that the inference seems clear that all proteins at some stage of their existence are fibrous in the molecular sense Recently [Astbury and Lomax, 1934, 1, 2; 1935] this concept has been expressed as a generalised interpretation of denaturation in the conclusion that the two more stable and insoluble states of protein structure, the fibrous and the denatured, are based on fundamentally similar modes of molecular arrangement; that, in fact, the denatured state2 is essentially a fibrous state inasmuch as it always consists of peptide chains, often fully extended, and aggregated after coagulation in parallel bundles, as in fibroin Plate V, Figs. ,B-Keratin is built from almost fully-extended polypeptide chains linked side-to-side, firstly by combinations between their side-chains ("side-chain linkage "), and secondly in a direction at right angles [Astbury and Sisson, 1935], through attractions between the =CO and =NH groups of neighbouring main-chains ("backbone linkage"). The three-dimensional structure is that of a pile of polypeptide "grids ", the average distance apart of the main-chains in the plane of each grid being about 9*8 A. ("side-chain spacing") and the distance between the grids being 4*65 A. (" backbone spacing "). These two spacings correspond respectively to the two reflections, 001 and 200, seen on the equator of Fig. Fig.

The major protein component of muscular tissue, myosin, has occupied the attention of many investigators because of its extreme importance as the contractile element of living. muscle. When isolated from the tissue it has many of the properties of the globulins, but its extreme molecular asymmetry gives rise to interesting properties which on the whole are anomalous to the corpuscular proteins. Past research has been devoted mainly to physico-chemical studies, and amongst these the investigation of double refraction of flow [Muralt & Edsall, 1930; Edsall & Mehl, 1940] and the interpretation of structure by X-ray methods [e.g. Boehm, 1931; 1933; Some work has also been carried out upon its solubillty [Bate