Water and biomolecules—physical chemistry of life: Kuwajima, K.; Goto, Y.; Hirata, F.; Terazima, M.; Kataoka, M. (eds.): Phenomena Series: Biological and Medical Physics, Biomedical Engineering, Springer (2009), XVIII, 307 p. 125 illus., 10 in color., Hardcover, ISBN 978-3-540-88786-7, €129.95
| Autor: | Rudolf Podgornik |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2010 |
| Předmět: |
chemistry.chemical_classification
Circular dichroism Goto Biomolecule Biophysics Cell Biology Atomic and Molecular Physics and Optics Book Review Folding (chemistry) chemistry Physical chemistry Protein folding Hydrophobic collapse Molecular Biology Protein secondary structure Heteronuclear single quantum coherence spectroscopy |
| Popis: | This book contains contributions from research associates of the Japanese Ministry of Education, Science, Culture, Sports and Technology on the research project “Water in Biomolecules” as well as several invited speakers from the final workshop of the project in the beginning of 2008. In 15 chapters and 307 pages, the book covers the physical chemistry of biological processes that involve the joint action of biomolecules and water, primarily in protein folding, dynamics, and function. By necessity, stemming from the proceedings of a single research project, it is a rather uneven and rugged overview of the field of synergy and interaction between biomolecules and water. Not all contributions in this volume are directly about water, but they are never far from it either. Nevertheless, the book contains some very interesting and well-written contributions to the physical chemistry of life processes that I can recommend to researchers working in this field. Some chapters also present extremely well-written overviews that would be interesting to read also for non-specialists. The first two chapters, viz. “Mapping Protein Folding Landscapes by NMR Relaxation” (P.E. Wright, D.J. Felitsky, K. Sugase, and H.J. Dyson) and “Experimental and Simulation Studies of the Folding/Unfolding of Goat α-Lactalbumin” (K. Kuwajima, T. Oroguchi, T. Nakamura, M. Ikeguchi, and A. Kidera) deal roughly with—nuclear magnetic resonance (NMR) in the former and circular dichroism (CD), fluorescence, and heteronuclear single quantum coherence spectroscopy in the latter—determination of the main features of the dynamics of the protein-folding process. Apomyoglobin is the subject of the first chapter, with specific attention being paid to the sites of local hydrophobic collapse, secondary structure formation, and transient long-range interactions via formation of transient hydrophobic contacts. Furthermore, an NMR relaxation study of coupled folding and binding of a disordered protein (pKID adsorption onto CBP) also shows that the folding–binding proceeds via the transient formation of hydrophobic contacts. The second chapter is centered on the folding and unfolding properties of authentic and recombinant forms of α-lactalbumin induced by GdnHCl concentration jumps and studied experimentally as well |
| Databáze: | OpenAIRE |
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