Protein Folding

Erscheinungsjahr 2027
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 Physik Angewandte Physik Biophysik
• Naturwissenschaften Biowissenschaften Molekularbiologie
• Naturwissenschaften Biowissenschaften Zellbiologie
• Naturwissenschaften Biowissenschaften Biochemie (nichtmedizinisch)

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
Professor Timir Tripathi is a Professor of Molecular Biology, School of Life Sciences, North-Eastern Hill University, Shillong, India. Earlier, he served as the Regional Director of Indira Gandhi National Open University. His previous role was Senior Assistant Professor and Principal Investigator at the Department of Biochemistry, NEHU, Shillong. He holds a Ph.D. from Jawaharlal Nehru University, New Delhi. His primary research focus is studying the conformational dynamics, interaction, and stabilization of the complexes formed by intrinsically disordered neuropathological protein aggregates, their properties of liquid-liquid phase separation, interaction, and roles in nucleocytoplasmic transport in neurodegenerative diseases. Professor Tripathi is an Associate Fellow of the Indian National Science Academy, New Delhi, and an elected member of the National Academy of Sciences, India, the Royal Society of Chemistry, and the Royal Society of Biology, UK