蛋白质高级结构专题课件.ppt

复旦大学生物化学系 黄伟达 The first three-dimensional structure of a biopolymer was the DNA model built by J. D. Watson and F. H. C. Crick in 1953 taking into account fiber diffraction data provided by M. H. F. Wilkins and others (Nobel Prize in Physiology or Medicine, 1962). Here is a copy of the original paper submitted to Nature on April 2, 1953 and published on April 25, 1953. The first three-dimensional protein structures (myoglobin and hemoglobin) were determined by M. F. Perutz and J. C. Kendrew (Nobel Prize in Chemistry, 1962). The entries included in the PDB (PDB codes: 1mbn and 2dhb) represent refined structures. J. C. Kendrew had obtained a myoglobin structure at a resolution of 6 A already in 1957. A. Klug has contributed substantially to the development of electron microscopy. This method is suitable for systems that cannot be crystallized (Nobel Prize in Chemistry, 1982). A. Klug has applied this method primarily to virus structures (see for example, Finch, Klug, J. Mol. Biol. 1965, 13, 1-12). The structure of the first membrane-bound protein (a photosynthetic reaction centre; PDB code: 1prc) was resolved by J. Deisenhofer, R. Huber and H. Michel (Nobel Prize in Chemistry, 1988). The first three-dimensional protein structure determined by NMR spectroscopy (proteinase IIa inhibitor from bull seminal plasma (PDB codes: 1bus, 2bus) was reported by K. Wüthrich and co-workers in 1985 (Nobel Prize in Chemistry, 2002). The “firsts” in macromolecule researches * * * * * * * * * * * * * 复旦大学生物化学系 黄伟达 By 1957, Kendrew had measured 400 reflections, and from them, created a structure for myoglobin at the level of 0.6 nm resolution. (No individual amino acid residues were visible) Later he analyzed 9600 reflections to produce a density map at 0.2 nm resolution. Finally, in 1962 he analyzed 25,000 reflections to produce a density map at 0.14 nm. Resolution of this level allowed assignment of 1200 of the 1260 non-hydrogen atoms. Today the technique of X-ray crystallo