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| David ParryDistinguished Professor of Biophysics
Qualifications and AchievementBSc(Hons) London (1963); PhD London (1966); DSc London (1982); Postdoctoral Fellow, Division of Protein Chemistry, CSIRO, Melbourne (1966-1969); Children's Cancer Research Foundation, Boston (1969-1971); Laboratory of Molecular Biophysics, Oxford (1971-1973); ICI Prize (1981); Fellow, NZ Institute of Chemistry (1983); Fellow, NZ Institute of Physics (1991); Fellow, Royal Society of NZ (1989). 2000 Hercus Medal from RSNZ , for his extended series of related studies of the chemistry, physics, biochemistry, ultrastructure and biological function of fibrous proteins. 2002 -elected Vice President of the International Council for Science (ICSU) at a recent meeting of the ICSU General Assembly in Rio de Janeiro. David is the first New Zealander to be appointed to this position and will be in charge of the Strategic Planning and Review portfolio. ICSU incorporates 27 Scientific Unions from 103 countries and covers all areas of science. Awarded the Shorland Medal by the New Zealand Association of Scientists (2006). The Shorland Medal is awarded for 'the significance and originality of a personal, life-time contribution to basic or applied research in New Zealand' . This recognises David's huge contribution to the study of biophysics in New Zealand. Massey University Research Medal for an outstanding individual researcher (2004); Distinguished Professor (2005). Head of Institute of Fundamental Sciences (1997-2006). Companion to the New Zealand Order of Merit (2007). Retired and returned on a part time research contract. RSNZ Rutherford Medal (2008). Research InterestsStructural BiophysicsMuch of my research work is collaborative and international in nature, and is concerned with the determination of the structure and function of fibrous biological macromolecules. X-ray diffraction and electron microscopy have been employed to ascertain structural details of the thin-filament regulatory mechanism in vertebrate skeletal muscle and of the growth, development and structure of collagen fibrils in a diverse range of connective tissues as a function of age. Also, computational and theoretical methods have been devised and employed to relate the amino acid sequence of a protein to its secondary, tertiary and quaternary structure. Towards that end our recent work has concentrated on the use of hydropathy profiles to recognise b-strands lying on the surface of proteins. Work in the sequence prediction area has provided details of the structure of the rod domain motif in the spectrin superfamily of proteins and on the structures of the interferons and interleukins, the desmoplakin superfamily of proteins, laminin, desmoyokin and the intermediate filaments. Crosslinking studies on the latter have allowed four related antiparallel modes of assembly to be characterised. Current plans centre on refining models for the structure of the N- and C- terminal domains of a hard α-keratin intermediate filament molecule. Additional work on the structure of α-internexin IF has now been completed. A major advance in the past year or so has been the detailed determination of the structure of the hair intermediate filament. We have shown that the expression and assembly of these intermediate filament proteins, which occurs under reducing conditions at a point just above the dermal papilla, leads to a structure that is very closely similar to that seen for other classes of intermediate filaments. However, when the intermediate filament associated proteins are laid down at a point higher in the hair follicle and conditions change to an oxidising one following cell death there is a significiant structural rearrangement of the constituent molecules. This leads to a unique structure. These observations have brought together a diverse group of experimental observations that previously seemed incompatible. Following on from these studies it has been possible to explain the different organization of sheets of IF in the para- and orthocortex of hair. |
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