LEADER 03489nam 2200589 a 450 001 9910830199803321 005 20230331005432.0 010 $a1-282-34774-8 010 $a9786612347740 010 $a0-470-51414-0 010 $a0-470-51415-9 035 $a(CKB)1000000000377098 035 $a(EBL)470469 035 $a(SSID)ssj0000307204 035 $a(PQKBManifestationID)11238217 035 $a(PQKBTitleCode)TC0000307204 035 $a(PQKBWorkID)10243797 035 $a(PQKB)11047975 035 $a(MiAaPQ)EBC470469 035 $a(OCoLC)181173376 035 $a(EXLCZ)991000000000377098 100 $a19910624d1991 uy 0 101 0 $aeng 135 $aur|n|---||||| 181 $ctxt 182 $cc 183 $acr 200 00$aProtein conformation$b[electronic resource] 210 $aChichester [England] ;$aNew York $cWiley$d1991 215 $a1 online resource (288 p.) 225 1 $aCiba Foundation symposium ;$v161 300 $aProceedings of the Symposium on Protein Conformation, held Jan. 22-24, 1991 at the Ciba Foundation, London, England. 300 $a"A Wiley-Interscience publication". 311 $a0-471-92969-7 320 $aIncludes bibliographical references and indexes. 327 $aPROTEIN 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 327 $aThe 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 327 $aExperimental studies of pathways of protein foldingProtein stability and protein folding; Ca2+ binding in proteins of the calmodulin superfamily: cooperativity, electrostatic contributions and molecular mechanisms; Protein-protein interaction: an analysis by computer simulation; General discussion; Index of contributors; Subject index 330 $aHow the amino acid sequence of a protein determines its three-dimensional structure is a major problem in biology and chemistry. Leading experts in the fields of NMR spectroscopy, X-ray crystallography, protein engineering and molecular modeling offer provocative insights into current views on the protein folding problem and various aspects for future progress. 410 0$aCiba Foundation symposium ;$v161. 606 $aProteins$xConformation$vCongresses 615 0$aProteins$xConformation 676 $a574.19 676 $a574.19245 712 12$aSymposium on Protein Conformation$f(1991 :$eCiba Foundation) 801 0$bMiAaPQ 801 1$bMiAaPQ 801 2$bMiAaPQ 906 $aBOOK 912 $a9910830199803321 996 $aProtein conformation$94082536 997 $aUNINA