Editor: Mario D. Galigniana

Series Title: Frontiers in Structural Biology

Role of Molecular Chaperones in Structural Folding, Biological Functions, and Drug Interactions of Client Proteins

Volume 1

eBook: US $89 Special Offer (PDF + Printed Copy): US $163
Printed Copy: US $119
Library License: US $356
ISSN: 2589-4366 (Print)
ISSN: 2589-4374 (Online)
ISBN: 978-1-68108-616-3 (Print)
ISBN: 978-1-68108-615-6 (Online)
Year of Publication: 2018
DOI: 10.2174/97816810861561180101


The book provides an updated panorama of the functional relevance of molecular chaperones in the proper folding of client factors, protein-protein interactions, the regulation of key biological functions, the development of ligand-based structural complexes and the consequent pharmacological or biotechnological applications of these processes. The involvement of molecular chaperones in several processes ranging from regulation of transcription factors and protein-protein interactions in bacteria to proteostasis, signaling pathways and cancer are also addressed. The book is an essential consulting tool for researchers, working professionals in academia or industry, and students of all levels who wish to obtain the most relevant and updated information currently available about protein folding and chaperones.


- Pp. i-ii (2)
Mario D. Galigniana
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List of Contributors

- Pp. iii-iv (2)
Mario D. Galigniana
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Regulatory Roles for Hsp70 in Cancer Incidence and Tumor Progression

- Pp. 1-22 (22)
Taka Eguchi, Benjamin J. Lang, Ayesha Murshid, Thomas Prince, Jianlin Gong, Stuart K Calderwood
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Use of Coarse-Grained and All-Atom Molecular Dynamics to Study Hsp70 and Hsp40 Chaperone Action

- Pp. 23-46 (24)
Ewa I. Gołas, Magdalena A. Mozolewska, Paweł Krupa, Cezary Czaplewski, Harold A. Scheraga, Adam Liwo
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Quaternary Structure of Chaperones from the Hsp70 System Determined by Small Angle X-Ray Scattering (SAXS) and Analytical Ultracentrifugation

- Pp. 47-72 (26)
Julio C. Borges, Carlos H.I. Ramos
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Structural Characteristics of the TPR Protein- Hsp90 Interaction: A New Target in Biotechnology

- Pp. 73-173 (101)
Ana Cauerhff, Mario D. Galigniana
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GroEL Chaperonin: Interaction with Polypeptides Lacking a Rigid Tertiary Structure

- Pp. 174-189 (16)
Victor V. Marchenkov, Natalia Yu Marchenko, Gennady V. Semisotnov
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Mechanisms of Protein Folding by Type II Chaperonins

- Pp. 190-213 (24)
Rebecca L. Plimpton, Jose M. Valpuesta, Barry M. Willardson
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Mechanisms and Functions of the Cytosolic DNAJHsp70 Chaperone System

- Pp. 214-250 (37)
Imad Baaklini, Jason C. Young
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Subject Index

- Pp. 252-265 (14)
Mario D. Galigniana
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