Robert Donald Bruce Fraser 1924–2019

2020 ◽  
Vol 31 (2) ◽  
pp. 157
Author(s):  
George E. Rogers ◽  
Andrew Miller ◽  
David A. D. Parry
Keyword(s):  
World Wide ◽  
Biological Molecules ◽  
Protein Chemistry ◽  
Birkbeck College ◽  
Instructor Training ◽  
Royal Air Force ◽  
Fibrous Proteins ◽  
Fibrous Protein ◽  
King's College ◽  
Part Time

Robert Donald Bruce (Bruce) Fraser was a biophysicist who gained world-wide distinction for his extensive structural studies of fibrous proteins. Bruce began a part-time BSc degree at Birkbeck College, London, while working as a laboratory assistant. In 1942, aged 18, he interrupted his studies and volunteered for training as a pilot in the Royal Air Force (RAF). He was sent to the Union of South Africa and was selected for instructor training, specialising in teaching pilot navigation. At the end of the war he completed his BSc at King’s College, London, and followed this with a PhD. Bruce studied the structure of biological molecules, including DNA, using infra-red micro-spectroscopy in the Biophysics Unit at King’s led by physicist J. T. Randall FRS. During that time Bruce built a structure for DNA that was close to the Watson-Crick structure that gained them and Maurice Wilkins at Kings College, the Nobel Prize in 1962. In 1952, he immigrated to Australia with his family to a position in the newly formed Wool Textile Research Laboratories at the Commonwealth Scientific and Industrial Research Organisation (CSIRO). Here, Bruce established a biophysics group for research on the structure of wool and other fibrous proteins that flourished until his retirement. Over that period he was internationally recognized as the pre-eminent fibrous protein structuralist world-wide. Having been acting chief, Bruce was subsequently appointed chief of the Division of Protein Chemistry and he remained in that role until he took retirement in 1987.

scholarly journals Structure and Identification of Solenin: A Novel Fibrous Protein from BivalveSolen grandisLigament

2014 ◽  
Vol 2014 ◽  
pp. 1-7
Author(s):  
Jun Meng ◽  
Gang-Sheng Zhang ◽  
Zeng-Qiong Huang
Keyword(s):  
Mechanical Performance ◽  
Type I ◽  
Fibrous Proteins ◽  
Repeat Sequences ◽  
Fibrous Protein ◽  
Secondary Structure Analysis ◽  
Solen Grandis ◽  
Opening And Closing ◽  
Insight Into

Fibrous proteins, which derived from natural sources, have been acting as templates for the production of new materials for decades, and most of them have been modified to improve mechanical performance. Insight into the structures of fibrous proteins is a key step for fabricating of bioinspired materials. Here, we revealed the microstructure of a novel fibrous protein: solenin fromSolen grandisligament and identified the protein by MALDI-TOF-TOF-MS and LC-MS-MS analyses. We found that the protein fiber has no hierarchical structure and is homologous to keratin type II cytoskeletal 1 and type I cytoskeletal 9-like, containing “SGGG,” “SYGSGGG,” “GS,” and “GSS” repeat sequences. Secondary structure analysis by FTIR shows that solenin is composed of 41.8%β-sheet, 16.2%β-turn, 26.5%α-helix, and 9.8% disordered structure. We believe that theβ-sheet structure and those repeat sequences which form “glycine loops” may give solenin excellence elastic and flexible properties to withstand tensile stress caused by repeating opening and closing of the shell valves in vivo. This paper contributes a novel fibrous protein for the protein materials world.

scholarly journals George Frederick James Temple, 2 September 1901 - 30 January 1992

1994 ◽  
Vol 40 ◽  
pp. 383-400 ◽  
Keyword(s):  
Elementary School ◽  
Mathematics Teachers ◽  
Scientific Activity ◽  
Research Assistant ◽  
Birkbeck College ◽  
The Third ◽  
Part Time ◽  
Great Western Railway ◽  
One Year ◽  
Physics Department

George Temple was born in London on 2 September 1901. There is no record of any previous scientific activity in his family; his father James Temple and his mother Frances ( née Compton) were country folk from Oxfordshire, although by the time George was born James was working for the Great Western Railway at Paddington Station. George himself stressed his good fortune in having three teachers of mathematics of outstanding ability, the first two being Ray Gilbert (who taught George briefly at Northfields Elementary School) and P. G. Goodall (at Ealing County School). James Temple’s death meant that George had to leave Ealing School after less than five years to seek employment. Within a year of leaving, however, he had enrolled as an evening student at Birkbeck College. He decided to study science rather than his other love, classics, and so met the third of his inspiring mathematics teachers, C. V. Coates. George was a student for only one year, 1918-19, after which Professor Albert Griffiths made him his part-time research assistant in physics, an appointment that freed George from his post at the Prudential Assurance Company, though with a cut in salary. It was at this time that he became a Catholic, and his strong faith informed the rest of his life. He had many close Dominican friends and learnt to value the theology of St Thomas highly. He took the General Honours B.Sc. in 1922 and became Steward in the Physics Department for two years.

Δ Protein, a New Fibrous Protein of Skeletal Muscle: Complex Formation With Myosin

1957 ◽  
Vol 188 (2) ◽  
pp. 219-226 ◽  
Author(s):  
Howard B. Bensusan ◽  
John I. White ◽  
Sylvia Himmelfarb ◽  
Brigitte E. Blankenhorn ◽  
William R. Amberson
Keyword(s):  
Skeletal Muscle ◽  
Complex Formation ◽  
Protein C ◽  
Protein A ◽  
Myosin Molecule ◽  
Fibrous Proteins ◽  
Fibrous Protein ◽  
Rapid Fall ◽  
Boundary Cell ◽  
Muscle Complex

A complex, Δ-myosin, is formed by the union of myosin with Δ protein. This complex may be demonstrated in several ways: a) it appears as a separate peak on the patterns of descending boundaries in electrophoresis, and has a mobility intermediate between the mobilities of myosin and D protein. b) It may be detected in the patterns of the ascending boundaries by the increase in the area of the myosin peak and the decrease in the area of free D protein. c) It may be seen in ultracentrifuge diagrams, and is best demonstrated in the synthetic boundary cell. In the mixtures of the three fibrous proteins, myosin, actin and Δ protein, it can be shown that Δ-myosin exists in the presence of an excess of actin. When isoviscous solutions of Δ protein and actomyosin are mixed, there is a rapid fall in viscosity. This fall indicates that some of the actomyosin has been dissociated. The Δ protein then unites with the free myosin to form Δ-myosin. Since Δ-myosin sediments more slowly than does the free myosin, and since the viscosity falls slightly when isoviscous solutions of Δ protein and myosin are mixed, we suggest that the myosin molecule is split during formation of the complex.

scholarly journals Philip Frank Wareing. 27 April 1914 — 29 March 1996

1999 ◽  
Vol 45 ◽  
pp. 507-518
Author(s):  
Michael A. Hall
Keyword(s):  
World War Ii ◽  
World War I ◽  
Civil Service ◽  
World War ◽  
Birkbeck College ◽  
University College ◽  
Part Time ◽  
The University ◽  
Assistant Lecturer

Philip Wareing was born in Leigh-on-Sea, Essex, and after World War I moved to Benfleet and then to Watford, where he received his schooling. After leaving school he entered the Civil Service and took his BSc at Birkbeck College, University of London, where he studied part-time. After service during World War II in the Royal Electrical and Mechanical Engineers, he took up a post as a demonstrator and then an assistant lecturer at Bedford College, University of London, obtaining his PhD in 1948. In 1950 he moved to the Department of Botany at Manchester and in 1958 he was appointed Professor of Botany in the University College of Wales, Aberystwyth, in which post he remained until his retirement in 1981.

Charles Wayne Rees CBE. 15 October 1927 — 21 September 2006

2015 ◽  
Vol 61 ◽  
pp. 351-378
Author(s):  
Christopher J. Moody
Keyword(s):  
Scientific Work ◽  
Building Blocks ◽  
Heterocyclic Chemistry ◽  
Birkbeck College ◽  
Heterocyclic Molecules ◽  
King's College ◽  
Naturally Occurring ◽  
Organic Chemist ◽  
Life Itself ◽  
The University

Charles Rees was an eminent organic chemist. He specialized in the area of heterocyclic chemistry—the study of rings made up of carbon, nitrogen, oxygen and sulphur atoms—an important subject given that many medicines, agrochemicals, dyes and reprographic materials, as well as a very large number of naturally occurring compounds, including the DNA bases, the building blocks of life itself, are heterocyclic molecules. His scientific work was dominated by two overarching themes: reactive intermediates, in particular neutral, electron-deficient species such as carbenes, nitrenes and arynes, and unusual ring systems, particularly strained rings and novel aromatic systems, including those rich in sulphur and nitrogen atoms. Born in 1927, he was educated at Farnham Grammar School, then spent three years at the Royal Aircraft Establishment, before going to University College Southampton (later Southampton University) (BSc 1950, PhD 1953). After a postdoctoral period, he was appointed assistant lecturer at Birkbeck College, London, in 1955, before moving to a lectureship at King’s College, London, and subsequently to chairs at the University of Leicester (1965), the University of Liverpool (1969) and Imperial College, London (1978). He was elected to the Royal Society in 1974 and appointed CBE in 1995. He died in London in 2006.

scholarly journals Histological analysis of elastic cartilages treated with alkaline solution

2020 ◽  
Vol 72 (3) ◽  
pp. 647-654
Author(s):  
K.D. Ferreira ◽  
L.D. Cardoso ◽  
L.P. Oliveira ◽  
V.S. Franzo ◽  
A. Pancotti ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Alkaline Solution ◽  
Histological Analysis ◽  
Elastic Fiber ◽  
Peripheral Region ◽  
Cell Counting ◽  
Elastic Fibers ◽  
Fibrous Proteins ◽  
Fibrous Protein ◽  
Areas Of Interest

ABSTRACT The elastic cartilage is composed by chondroblasts and chondrocytes, extracellular matrix and surrounded by perichondrium. It has a low regeneration capacity and is a challenge in surgical repair. One of obstacles in engineering a structurally sound and long-lasting tissue is selecting the most appropriate scaffold material. One of the techniques for obtaining biomaterials from animal tissues is the decellularization that decreases antigenicity. In this work, alkaline solution was used in bovine ear elastic cartilages to evaluate the decellularization and the architecture of the extracellular matrix. The cartilages were treated in alkaline solution (pH13) for 72 hours and lyophilized to be compared with untreated cartilages by histological analysis (hematoxylin-eosin, Masson's trichrome and Verhoeff slides). Areas of interest for cell counting and elastic fiber quantification were delineated, and the distribution of collagen and elastic fibers and the presence of non-fibrous proteins were observed. The results demonstrated that the alkaline solution caused 90% decellularization in the middle and 13% in the peripheral region, and maintenance of the histological characteristics of the collagen and elastic fibers and non-fibrous protein removal. It was concluded that the alkaline solution was efficient in the decellularization and removal of non-fibrous proteins from the elastic cartilages of the bovine ear.

Sign in / Sign up

Export Citation Format

Share Document