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[null,"1.","Record Nr.",null,"UNINA9910144564203321"]
[null,null,"Titolo",null,"Protein conformation [[electronic resource]]"]
[null,null,"Pubbl/distr/stampa",null,"Chichester [England] ; ; New York, : Wiley, 1991"]
[null,null,"ISBN",null,"1-282-34774-8"]
[{"$nulls":4},"9786612347740"]
[{"$nulls":4},"0-470-51414-0"]
[{"$nulls":4},"0-470-51415-9"]
[null,null,"Descrizione fisica",null,"1 online resource (288 p.)"]
[null,null,"Collana",null,"Ciba Foundation symposium ; ; 161"]
[null,null,"Disciplina",null,"574.19"]
[{"$nulls":4},"574.19245"]
[null,null,"Soggetti",null,"Proteins - Conformation"]
[{"$nulls":4},"Electronic books."]
[null,null,"Lingua di pubblicazione",null,"Inglese"]
[null,null,"Formato",null,"Materiale a stampa"]
[null,null,null,"Livello bibliografico","Monografia"]
[null,null,null,"Note generali","Proceedings of the Symposium on Protein Conformation, held Jan. 22-24, 1991 at the Ciba Foundation, London, England."]
[{"$nulls":4},"\"A Wiley-Interscience publication\"."]
[null,null,null,"Nota di bibliografia","Includes bibliographical references and indexes."]
[null,null,"Nota di contenuto",null,"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"]
[{"$nulls":4},"The application of computational methods to the study of enzyme catalysis by triose-phosphate isomerase and stabilities of variants of bacteriophage T4 lysozymeMultidimensional triple resonance NMR spectroscopy of isotopically uniformly enriched proteins: a powerful new strategy for structure determination; Six years of protein structure determination by NMR spectroscopy: what have we learned?; On deriving spatial protein structure from NMR or X-ray diffraction data; NMR spectroscopy and protein folding: studies of lysozyme and a-lactalbumin"]
[{"$nulls":4},"Experimental studies of pathways of protein foldingProtein stability and protein folding; Ca2+ binding in proteins of the calmodulin superfamily: cooperativity, electrostatic contributions and molecular "]
[{"$nulls":4},"mechanisms; Protein-protein interaction: an analysis by computer simulation; General discussion; Index of contributors; Subject index"]
[null,null,null,"Sommario/riassunto","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."]