Protein structural analysis, folding and design
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Bibliographic Information
Protein structural analysis, folding and design
Japan Scientific Societies Press , Elsevier, 1990
- : Japan
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Description and Table of Contents
Description
Our understanding of the structure-function relationship in proteins was revolutionized in the 1980's by the use of site-directed mutagenesis coupled with X-ray crystallography, which reveals the story of protein functions in their atomic resolution. This was still limited, however, to the hydrolytic enzymes hemoproteins such as myoglobin and hemoglobin. Our knowledge of protein-functions is also being increased through such computer-aided approaches as graphic design and molecular mechanics, although these approaches too are currently applicable for smaller proteins. From 1986 to 1988 a group of Japanese scientists pursued research on the structural analyses, folding and design of various types of proteins including cytochrome P450, ferredoxins, hemoglobin, erbutoxin, neurotoxins, tryptophan synthase, thermophile isopropylmaleate dehydrogenase, fatty acid synthetase, ion-channel proteins and abnormal hemoglobins. Their findings are summarized in this volume, providing data on the capability and potential of site-directed mutagenesis, mutations in nature, and computer-aided predictions for more complicated proteins.
Table of Contents
Preface. I. Protein Structural Analysis and Folding . Protein Confirmation in Terms of Conformational Energy Analysis (H. Wako). Some Remarks on Protein Folding (N. Saito, K. Yura and Y. Fukuda). Postsynaptic Snake Neurotoxin: A Flexible Protein That Binds to the Acetylcholine Receptor (T. Endo and N. Tamiya). Characterization of the Folding Intermediates of Globular Proteins (S. Sugai, K. Kuwajima and K. Nitta). Physical and Biological Stability of Globular Proteins (S. Kidokoro, Y. Miki and A. Wada). Refined Structure of a [2Fe-2S] Ferredoxin I from Aphanothece sacrum: Intramolecular Interaction and Structural Organization (T. Tsukihara, K. Fukuyama, H. Matsubara and Y. Katsube). II. Higher-Order Structure of Protein Systems . Compound Function and Higher-Order Structure of Animal Fatty Acid Synthetase (H. Kyushiki, T. Kitamoto and A. Ikai). Denaturation of Membrane Proteins: Ion Channel, Calcium-ATPase and Baacteriorhodopsin (S. Mitaku, F. Kukita and M. Kasai). Clusterization of Proteins in Solution under Velocity Gradient of Solvent Flow (F. Hirakawa, S. Yoshino, M. Sogami and N. Imai). III. Mutation and Structural Design of Proteins. Molecular Physiology and Pathology of Hemoglobin M (M. Nagai and Y. Yoneyama). The Role of the Distal Residues of Haemoglobin (J. Tame). Manipulation of Hemoglobin Function by Protein Engineering (K. Imai, K. Ishimori, K. Fushitani, G. Miyazaki, T. Kitagawa, Y. Wada, H. Morimoto, I. Morishima, D. Shih, J. Tame and K. Nagai). Site-Directed Mutagenesis of Rat Liver Cytochrome P-450 d (M. Hatano, T. Shimizu, O. Ito, K. Hirano, H. Furuya, A.J. Md. Sadeque, Y. Fujii-Kuriyama, R. Raag and T.L. Poulos). Conformational Stability of Mutant Tryptophan Synthase alpha-Subunit (K. Yutani and K. Ogasawara). Subject Index. Imprint: Amsterdam/JSSP
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