1.

Record Nr.

UNINA9910144564203321

Titolo

Protein conformation [[electronic resource]]

Pubbl/distr/stampa

Chichester [England] ; ; New York, : Wiley, 1991

ISBN

1-282-34774-8

9786612347740

0-470-51414-0

0-470-51415-9

Descrizione fisica

1 online resource (288 p.)

Collana

Ciba Foundation symposium ; ; 161

Disciplina

574.19

574.19245

Soggetti

Proteins - Conformation

Electronic books.

Lingua di pubblicazione

Inglese

Formato

Materiale a stampa

Livello bibliografico

Monografia

Note generali

Proceedings of the Symposium on Protein Conformation, held Jan. 22-24, 1991 at the Ciba Foundation, London, England.

"A Wiley-Interscience publication".

Nota di bibliografia

Includes bibliographical references and indexes.

Nota di contenuto

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 superfamily: cooperativity, electrostatic contributions and molecular mechanisms; Protein-protein interaction: an analysis by computer simulation; General discussion; Index of contributors; Subject index

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.