Frontiers in Protein Structure, Function, and Dynamics (Hardcover, 1st ed. 2020)

This book discusses a broad range of basic and advanced topics in the field of protein structure, function, folding, flexibility, and dynamics. Starting with a basic introduction to protein purification, estimation, storage, and its effect on the protein structure, function, and dynamics, it also discusses various experimental and computational structure determination approaches; the importance of molecular interactions and water in protein stability, folding and dynamics; kinetic and thermodynamic parameters associated with protein-ligand binding; single molecule techniques and their applications in studying protein folding and aggregation; protein quality control; the role of amino acid sequence in protein aggregation; muscarinic acetylcholine receptors, antimuscarinic drugs, and their clinical significances. Further, the book explains the current understanding on the therapeutic importance of the enzyme dopamine beta hydroxylase; structural dynamics and motions in molecular motors; role of cathepsins in controlling degradation of extracellular matrix during disease states; and the important structure-function relationship of iron-binding proteins, ferritins. Overall, the book is an important guide and a comprehensive resource for understanding protein structure, function, dynamics, and interaction.

General

Imprint:	Springer Verlag, Singapore
Country of origin:	Singapore
Release date:	July 2020
First published:	2020
Editors:	Dev Bukhsh Singh • Timir Tripathi
Dimensions:	235 x 155mm (L x W)
Format:	Hardcover
Pages:	452
Edition:	1st ed. 2020
ISBN-13:	978-981-15-5529-9
Categories:	Books > Medicine > Pre-clinical medicine: basic sciences > Medical genetics Books > Science & Mathematics > Biology, life sciences > Molecular biology Books > Science & Mathematics > Biology, life sciences > Biochemistry > Proteins Books > Science & Mathematics > Biology, life sciences > Biochemistry > Enzymology
LSN:	981-15-5529-X
Barcode:	9789811555299

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