Protein conformation.
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 p...
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Corporate Authors: | , |
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Other Authors: | , |
Format: | Electronic Conference Proceeding eBook |
Language: | English |
Published: |
Chichester, England ; New York :
Wiley,
1991.
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Series: | Ciba Foundation symposium ;
161. |
Subjects: | |
Online Access: | CONNECT |
MARC
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111 | 2 | |a Symposium on Protein Conformation |d (1991 : |c Ciba Foundation) | |
245 | 1 | 0 | |a Protein conformation. |
260 | |a Chichester, England ; |a New York : |b Wiley, |c 1991. | ||
300 | |a 1 online resource (xii, 269 pages) : |b illustrations (some color) | ||
336 | |a text |b txt |2 rdacontent | ||
337 | |a computer |b c |2 rdamedia | ||
338 | |a online resource |b cr |2 rdacarrier | ||
490 | 1 | |a Ciba Foundation symposium ; |v 161 | |
500 | |a Wiley EBA |5 TMurS | ||
500 | |a Editors: Derek J. Chadwick and Kate Widdows. | ||
504 | |a Includes bibliographical references and indexes. | ||
505 | 0 | |a Mechanisms of enzyme catalysis from crystal structure analyses / G.E. Schulz -- Comparative analysis of protein three-dimensional structures and an approach to the inverse folding problem / T.L. Blundell -- Structural and genetic analysis of electrostatic and other interactions in bacteriophage T4 lysozyme / S. Dao-pin [and others] -- Simulation analysis of the stability mutants R96H of bacteriophage T4 lysozyme and 196A of barnase / M. Karplus [and others] -- Towards time-resolved diffraction studies with glycogen phosphorylase / E.M.H. Duke [and others] -- The application of computational methods to the study of enzyme catalysis by triose-phosphate isomerase and stabilities of variants of bacteriophage T4 lysozyme / P.A. Kollman, V. Daggett and L.X. Dang -- Multidimensional triple resonance NMR spectroscopy of isotopically uniformly enriched proteins : a powerful new strategy for structure determination / A. Bax [and others] -- Six years of protein structure determination by NMR spectroscopy : what have we learned? / K. Wüthrich -- On deriving spatial protein structure from NMR or X-ray diffraction data / W.F. van Gunsteren [and others] -- NMR spectroscopy and protein folding : studies of lysozyme and [alpha]-lactalbumin / C.M. Dobson -- Experimental studies of pathways of protein folding / R.L. Baldwin -- Protein stability and protein folding / R. Jaenicke -- Ca² binding in proteins of the calmodulin superfamily : cooperativity, electrostatic contributions and molecular mechanisms / S. Forsén [and others] -- Protein-protein interaction : an analysis by computer simulation / S. Duquerroy, J. Cherfils and J. Janin. | |
588 | 0 | |a Print version record. | |
533 | |a Electronic reproduction. |b [Place of publication not identified] : |c HathiTrust Digital Library, |d 2010. |5 MiAaHDL | ||
520 | |a 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. | ||
546 | |a English. | ||
650 | 0 | |a Proteins |x Conformation |v Congresses. | |
650 | 0 | |a Proteins |x Conformation. | |
650 | 0 | |a Proteins |x Conformation |x Congresses. | |
650 | 2 | |a Protein Conformation | |
655 | 2 | |a Congress | |
700 | 1 | |a Chadwick, Derek. | |
700 | 1 | |a Widdows, Kate. | |
710 | 2 | |a Ciba Foundation. | |
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