Protein Folding

Erscheinungsjahr 2026
ISBN: 978-0-443-45315-1
Verlag: Elsevier Science

Buch, Englisch, 250 Seiten, Format (B × H): 191 mm x 235 mm, Gewicht: 449 g

Protein Folding explores the fundamental and applied aspects of protein folding, misfolding, and stability in biological systems. Focusing on the biochemical principles and molecular dynamics that drive folding processes, the book provides readers with a comprehensive understanding of how proteins attain their native structures and what happens when this process goes awry. Covering diverse approaches from structural biology, biophysics, enzymology, and systems biology, the book highlights the molecular basis of folding pathways and the pathological consequences of misfolded proteins in diseases such as Alzheimer's, Parkinson's, and cystic fibrosis. It integrates insights into chaperone function, folding kinetics, and the cellular quality control mechanisms that safeguard proteostasis. Across its chapters, the book addresses key themes including protein folding landscapes, folding intermediates, the role of cellular compartments, aggregation-prone sequences, and the impact of mutations. It also examines current methodologies for studying protein folding, including spectroscopy, calorimetry, and computational simulations, and considers emerging therapeutic strategies that target misfolding and aggregation. This book is a valuable resource for biochemists, molecular biologists, biotechnologists, enzymologists, and researchers in protein science. It supports academic researchers, postgraduate students, and pharmaceutical scientists working to understand protein behavior and develop interventions for protein misfolding diseases.

Autoren/Hrsg.

Tripathi, Timir

Fachgebiete

• Naturwissenschaften Biowissenschaften Biochemie (nichtmedizinisch)
• Naturwissenschaften Biowissenschaften Molekularbiologie
• Naturwissenschaften Physik Angewandte Physik Biophysik
• Naturwissenschaften Biowissenschaften Zellbiologie

Inhaltsverzeichnis

1. Introduction to Protein Folding
2. Theoretical Frameworks in Protein Folding
3. Role of Molecular Chaperones in Folding
4. Protein Folding Inside Cells
5. Protein Folding Intermediates
6. Folding and Enzymatic Activity
7. Folding and Stability of Membrane Proteins
8. Folding Pathways of Multi-domain Proteins
9. Folding and Stability of Extremophilic Proteins
10. Intrinsically Disordered Proteins: A Paradigm Shift
11. Experimental and Computational Approaches to Study Protein Folding
12. Perspectives and Future Directions in Protein Folding Research

Über Autor(innen)

Tripathi, Timir
Dr. Timir Tripathi is a Professor of Molecular Biology, School of Life Sciences, North-Eastern Hill University, Shillong, India. He previously held positions as Regional Director of IGNOU in Kohima and a Senior Assistant Professor in the Department of Biochemistry at NEHU. His research focuses on protein–substrate interactions, conformational dynamics, and the regulatory roles of non-catalytic domains. He is especially interested in intrinsically disordered and phase-separated proteins, their roles in disease, and, more recently, molecular memory, adaptive learning, and intelligence in proteins. Professor Tripathi has received several awards and is an Associate Fellow of the Indian National Science Academy, New Delhi, and an elected member of the National Academy of Sciences, India. He is a section editor of Elsevier's International Journal of Biological Macromolecules and has published five books with Elsevier.