Robert Donald Bruce Fraser 1924–2019
George E. Rogers A , Andrew Miller B and David A. D. Parry C D
+ Author Affiliations
- Author Affiliations
A School of Biological Sciences, University of Adelaide, South Australia 5005, Australia.
B General Council Business Committee, University of Edinburgh, Charles Stewart House, 9–16 Chambers Street, Edinburgh EH1 1HT, Scotland.
C School of Fundamental Sciences, Massey University, Private Bag 11–222, Palmerston North 4442, New Zealand.
D Corresponding author. Email: d.parry@massey.ac.nz
Historical Records of Australian Science 31(2) 157-168 https://doi.org/10.1071/HR19015
Published: 3 June 2020
Abstract
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.
References
Cohen, C., and Holmes, K. C. (1963) X-ray diffraction evidence for α-helical coiled-coils in native muscle, Journal of Molecular Biology, 6, 423–432.| X-ray diffraction evidence for α-helical coiled-coils in native muscleCrossref | GoogleScholarGoogle Scholar | 14022021PubMed |
Filshie, B. K., and Rogers, G. E. (1961) The fine structure of α-keratin, Journal of Molecular Biology, 3, 784–786.
| The fine structure of α-keratinCrossref | GoogleScholarGoogle Scholar | 13892902PubMed |
Fraser, R. D. B. (2004) The structure of deoxyribose nucleic acid, Journal of Structural Biology, 145, 184–186.
| The structure of deoxyribose nucleic acidCrossref | GoogleScholarGoogle Scholar |
Fraser, R. D. B., and MacRae, T. P. (1959) Molecular organization in feather keratin, Journal of Molecular Biology, 1, 387–397.
| Molecular organization in feather keratinCrossref | GoogleScholarGoogle Scholar |
Fraser, R. D. B., and MacRae, T. P. (1963) Structural organization in feather keratin, Journal of Molecular Biology, 7, 272–280.
| Structural organization in feather keratinCrossref | GoogleScholarGoogle Scholar |
Fraser, R. D. B., and MacRae, T. P. (1971) Structure of alpha keratin, Nature, 233, 138–140.
| Structure of alpha keratinCrossref | GoogleScholarGoogle Scholar |
Fraser, R. D. B., and MacRae, T. P. (1973) Conformation in Fibrous Proteins and Related Synthetic Polypeptides, New York.
Fraser, R. D. B., and MacRae, T. P. (1976) ‘The molecular structure of feather keratin’, in Proceedings of the 16th International Ornithological Congress, eds. H. J. Frith and J. H. Calaby, Canberra, pp. 443–451.
Fraser, R. D. B., and MacRae, T. P. (1983) The structure of the α-keratin microfibril, Bioscience Reports, 3, 517–525.
| The structure of the α-keratin microfibrilCrossref | GoogleScholarGoogle Scholar |
Fraser, R. D. B., and MacRae, T. P. (1985) Intermediate filament structure, Bioscience Reports, 5, 573–579.
| Intermediate filament structureCrossref | GoogleScholarGoogle Scholar |
Fraser, R. D. B., and Parry, D. A. D. (1996) The molecular structure of reptilian keratin, International Journal of Biological Macromolecules, 19, 207–211.
| The molecular structure of reptilian keratinCrossref | GoogleScholarGoogle Scholar |
Fraser, R. D. B., and Parry, D. A. D. (2003) Macrofibril assembly in trichocyte hard α-keratins, Journal of Structural Biology, 142, 319–325.
| Macrofibril assembly in trichocyte hard α-keratinsCrossref | GoogleScholarGoogle Scholar |
Fraser, R. D. B., and Parry, D. A. D. (2008) Molecular packing in the feather keratin filament, Journal of Structural Biology, 162, 1–13.
| Molecular packing in the feather keratin filamentCrossref | GoogleScholarGoogle Scholar |
Fraser, R. D. B., and Parry, D. A. D. (2011a) The structural basis of the filament-matrix texture in the avian/reptilian group of hard β-keratins, Journal of Structural Biology, 173, 391–405.
| The structural basis of the filament-matrix texture in the avian/reptilian group of hard β-keratinsCrossref | GoogleScholarGoogle Scholar |
Fraser, R. D. B., and Parry, D. A. D. (2011b) The structural basis of the two-dimensional net pattern observed in the X-ray diffraction pattern of avian keratin, Journal of Structural Biology, 176, 340–349.
| The structural basis of the two-dimensional net pattern observed in the X-ray diffraction pattern of avian keratinCrossref | GoogleScholarGoogle Scholar |
Fraser, R. D. B., and Parry, D. A. D. (2012) The role of disulphide bond formation in the structural transition observed in the intermediate filaments of the developing hair, Journal of Structural Biology, 180, 117–124.
| The role of disulphide bond formation in the structural transition observed in the intermediate filaments of the developing hairCrossref | GoogleScholarGoogle Scholar |
Fraser, R. D. B., and Parry, D. A. D. (2014a) Keratin intermediate filaments: differences in the sequences of the type I and type II chains explain the origin of the stability of an enzyme-resistant four-chain fragment, Journal of Structural Biology, 185, 317–326.
| Keratin intermediate filaments: differences in the sequences of the type I and type II chains explain the origin of the stability of an enzyme-resistant four-chain fragmentCrossref | GoogleScholarGoogle Scholar |
Fraser, R. D. B., and Parry, D. A. D. (2014b) Amino acid sequence homologies in the hard keratins of birds and reptiles, and their implications for molecular structure and physical properties, Journal of Structural Biology, 188, 213–224.
| Amino acid sequence homologies in the hard keratins of birds and reptiles, and their implications for molecular structure and physical propertiesCrossref | GoogleScholarGoogle Scholar |
Fraser, R. D. B., and Parry, D. A. D. (2017) Intermediate filament structure in the fully differentiated (oxidised) trichocyte keratin, Journal of Structural Biology, 200, 45–53.
| Intermediate filament structure in the fully differentiated (oxidised) trichocyte keratinCrossref | GoogleScholarGoogle Scholar |
Fraser, R. D. B., and Parry, D. A. D. (2018a) Direct evidence supporting the existence of a helical dislocation in protofilament packing in the intermediate filaments of oxidized trichocyte keratin, Journal of Structural Biology, 204, 491–497.
| Direct evidence supporting the existence of a helical dislocation in protofilament packing in the intermediate filaments of oxidized trichocyte keratinCrossref | GoogleScholarGoogle Scholar |
Fraser, R. D. B., and Parry, D. A. D. (2018b) ‘Structural hierarchy of trichocyte keratin intermediate filaments’, in The Hair Fibre: Proteins, Structure and Development, Advances in Experimental Medicine and Biology vol. 1054, eds. J. Plowman, D. Harland, S. Deb-Choudhury, Singapore, pp. 57–70.
Fraser, R. D. B., and Parry, D. A. D. (2020) Lepidosaur β-keratin chains with four 34-residue repeats: modelling reveals a potential filament cross-linking role, Journal of Structural Biology, 209, 107413.
| Lepidosaur β-keratin chains with four 34-residue repeats: modelling reveals a potential filament cross-linking roleCrossref | GoogleScholarGoogle Scholar |
Fraser, R. D. B., and Suzuki, E. (1965) Polypeptide chain conformation in feather keratin, Journal of Molecular Biology, 14, 279–282.
| Polypeptide chain conformation in feather keratinCrossref | GoogleScholarGoogle Scholar |
Fraser, R. D. B., Miller, A., and MacRae, T. P. (1964a) Fourier transform of assembly of helices, Acta Crystallographica, 17, 769–770.
| Fourier transform of assembly of helicesCrossref | GoogleScholarGoogle Scholar |
Fraser, R. D. B., Miller, A., and MacRae, T. P. (1964b) Fourier transform of coiled-coil model for alpha keratin, Acta Crystallographica, 17, 813–816.
| Fourier transform of coiled-coil model for alpha keratinCrossref | GoogleScholarGoogle Scholar |
Fraser, R. D. B., MacRae, T. P., and Miller, A. (1964c) Molecular structure of α-keratin, Nature, 203, 1231–1233.
| Molecular structure of α-keratinCrossref | GoogleScholarGoogle Scholar |
Fraser, R. D. B., MacRae, T. P., and Miller, A. (1965) X-ray diffraction pattern of α-fibrous proteins, Journal of Molecular Biology, 14, 432–442.
| X-ray diffraction pattern of α-fibrous proteinsCrossref | GoogleScholarGoogle Scholar |
Fraser, R. D. B., MacRae, T. P., and Parry, D. A. D. (1968) ‘The substructure of the α-keratin microfibril’ in Symposium on Fibrous Proteins (Australia 1967), ed. W. G. Crewther, Sydney, pp. 279–286.
Fraser, R. D. B., MacRae, T. P., Parry, D. A. D., and Suzuki, E. (1971) The structure of feather keratin, Polymer, 12, 35–56.
| The structure of feather keratinCrossref | GoogleScholarGoogle Scholar |
Fraser, R. D. B., MacRae, T. P., Miller, A., and Rowlands, R. J. (1976) Digital processing of fiber diffraction patterns, Journal of Applied Crystallography, 9, 81–94.
| Digital processing of fiber diffraction patternsCrossref | GoogleScholarGoogle Scholar |
Fraser, R. D. B., MacRae, T. P., Miller, A., and Suzuki, E. (1983) Molecular conformation and packing in collagen fibrils, Journal of Molecular Biology, 167, 497–521.
| Molecular conformation and packing in collagen fibrilsCrossref | GoogleScholarGoogle Scholar |
Fraser, R. D. B., Rogers, G. E., and Parry, D. A. D. (2003a) Nucleation and growth of macrofibrils in trichocyte (hard-α) keratins, Journal of Structural Biology, 143, 85–93.
| Nucleation and growth of macrofibrils in trichocyte (hard-α) keratinsCrossref | GoogleScholarGoogle Scholar |
Fraser, R. D. B., Steinert, P. M., and Parry, D. A. D. (2003b) Structural changes in trichocyte keratin intermediate filaments during keratinization, Journal of Structural Biology, 142, 266–271.
| Structural changes in trichocyte keratin intermediate filaments during keratinizationCrossref | GoogleScholarGoogle Scholar |
Hodgkin, D. M. C. (1980) John Desmond Bernal. 10 May–15 September 1971, Biographical Memoirs of Fellows of the Royal Society. Royal Society (Great Britain), 26, 16–84.
| John Desmond Bernal. 10 May–15 September 1971Crossref | GoogleScholarGoogle Scholar |
Hulmes, D. J. S., and Miller, A. (1979) Quasi-hexagonal molecular packing in collagen fibrils, Nature, 282, 878–880.
| Quasi-hexagonal molecular packing in collagen fibrilsCrossref | GoogleScholarGoogle Scholar |
Miller, A. (1984) Collagen – The organic matrix of bone, Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences, 304, 455–477.
| Collagen – The organic matrix of boneCrossref | GoogleScholarGoogle Scholar | 6142488PubMed |
North, A. C. T., Cowan, P. M., and Randall, J. T. (1954) Structural units in collagen fibrils, Nature, 174, 1142–1143.
| Structural units in collagen fibrilsCrossref | GoogleScholarGoogle Scholar |
Parry, D. A. D. (2014) Fifty years of fibrous protein research: a personal retrospective, Journal of Structural Biology, 186, 320–334.
| Fifty years of fibrous protein research: a personal retrospectiveCrossref | GoogleScholarGoogle Scholar |
Parry, D. A. D., Fraser, R. D. B., and Squire, J. M. (2008) Fifty years of coiled-coils and α-helical bundles: a close relationship between sequence and structure, Journal of Structural Biology, 163, 258–269.
| Fifty years of coiled-coils and α-helical bundles: a close relationship between sequence and structureCrossref | GoogleScholarGoogle Scholar |
Parry, D. A. D., Fraser, R. D. B., Alibardi, L., Rutherford, K. M., and Gemmell, N. (2019) Molecular structure of sauropsid β-keratins from tuatara (Sphenodon punctatus), Journal of Structural Biology, 207, 21–28.
| Molecular structure of sauropsid β-keratins from tuatara (Sphenodon punctatus)Crossref | GoogleScholarGoogle Scholar |
Rivett, D. E., Ward, C. W., Belkin, L. M., Ramshaw, J. A. M., and Wilshire, J. F. K. (1996) The Lennox Legacy: the History of the CSIRO Laboratory at 343 Royal Parade Parkville, Collingwood.
Rogers, G. E. (1959) Electron microscopy of wool, Journal of Ultrastructure Research, 2, 309–330.
| Electron microscopy of woolCrossref | GoogleScholarGoogle Scholar | 13655351PubMed |
Smith, J. W. (1968) Molecular pattern in native collagen, Nature, 219, 157–158.
| Molecular pattern in native collagenCrossref | GoogleScholarGoogle Scholar | 4173353PubMed |
Steinert, P. M., Marekov, L. N., Fraser, R. D. B., and Parry, D. A. D. (1993) Keratin intermediate filament structure: crosslinking studies yield quantitative information on molecular dimensions and mechanism of assembly, Journal of Molecular Biology, 230, 436–452.
| Keratin intermediate filament structure: crosslinking studies yield quantitative information on molecular dimensions and mechanism of assemblyCrossref | GoogleScholarGoogle Scholar | 7681879PubMed |
Wang, H., Parry, D. A. D., Jones, L. N., Idler, W. W., Marekov, L. N., and Steinert, P. M. (2000) In vitro assembly and structure of trichocyte keratin intermediate filaments: a novel role for stabilization by disulphide linkages, The Journal of Cell Biology, 151, 1459–1468.
| In vitro assembly and structure of trichocyte keratin intermediate filaments: a novel role for stabilization by disulphide linkagesCrossref | GoogleScholarGoogle Scholar | 11134075PubMed |
