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Record Nr. |
UNINA9910876503203321 |
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Titolo |
Protein conformation |
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Pubbl/distr/stampa |
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Chichester [England] ; ; New York, : Wiley, 1991 |
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ISBN |
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1-282-34774-8 |
9786612347740 |
0-470-51414-0 |
0-470-51415-9 |
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Descrizione fisica |
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1 online resource (288 p.) |
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Collana |
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Ciba Foundation symposium ; ; 161 |
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Disciplina |
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Soggetti |
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Lingua di pubblicazione |
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Formato |
Materiale a stampa |
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Livello bibliografico |
Monografia |
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Note generali |
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Proceedings of the Symposium on Protein Conformation, held Jan. 22-24, 1991 at the Ciba Foundation, London, England. |
"A Wiley-Interscience publication". |
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Nota di bibliografia |
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Includes bibliographical references and indexes. |
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Nota di contenuto |
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PROTEIN CONFORMATION; Contents; Introduction; Mechanisms of enzyme catalysis from crystal structure analyses; Comparative analysis of protein three-dimensional structures and an approach to the inverse folding problem; Structural and genetic analysis of electrostatic and other interactions in bacteriophage T4 lysozyme; Simulation analysis of the stability mutants R96H of bacteriophage T4 lysozyme and I96A of barnase; Towards time-resolved diffraction studies with glycogen phosphorylase |
The application of computational methods to the study of enzyme catalysis by triose-phosphate isomerase and stabilities of variants of bacteriophage T4 lysozymeMultidimensional triple resonance NMR spectroscopy of isotopically uniformly enriched proteins: a powerful new strategy for structure determination; Six years of protein structure determination by NMR spectroscopy: what have we learned?; On deriving spatial protein structure from NMR or X-ray diffraction data; NMR spectroscopy and protein folding: studies of lysozyme and a-lactalbumin |
Experimental studies of pathways of protein foldingProtein stability and protein folding; Ca2+ binding in proteins of the calmodulin |
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superfamily: cooperativity, electrostatic contributions and molecular mechanisms; Protein-protein interaction: an analysis by computer simulation; General discussion; Index of contributors; Subject index |
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Sommario/riassunto |
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How the amino acid sequence of a protein determines its three-dimensional structure is a major problem in biology and chemistry. Leading experts in the fields of NMR spectroscopy, X-ray crystallography, protein engineering and molecular modeling offer provocative insights into current views on the protein folding problem and various aspects for future progress. |
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