1.

Record Nr.

UNINA9910794778103321

Autore

DAM工作室

Titolo

VVIP高端会所设计2(DAM工作室)

Pubbl/distr/stampa

Huazhong, : Huazhong University of Science and Technology Press, 2014

ISBN

7-5609-9556-X

Descrizione fisica

1 online resource (320 p.)

Lingua di pubblicazione

Cinese

Formato

Materiale a stampa

Livello bibliografico

Monografia

Note generali

Description based upon print version of record.

Nota di contenuto

Pages:1 to 25; Pages:26 to 50; Pages:51 to 75; Pages:76 to 100; Pages:101 to 125; Pages:126 to 150; Pages:151 to 175; Pages:176 to 200; Pages:201 to 225; Pages:226 to 250; Pages:251 to 275; Pages:276 to 300; Pages:301 to 320



2.

Record Nr.

UNINA9911019225803321

Titolo

Protein conformation

Pubbl/distr/stampa

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

ISBN

9786612347740

9781282347748

1282347748

9780470514146

0470514140

9780470514153

0470514159

Descrizione fisica

1 online resource (288 p.)

Collana

Ciba Foundation symposium ; ; 161

Disciplina

574.19/245

Soggetti

Proteins - Conformation

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.