| Description |
1 online resource (xiii, 327 pages) : illustrations |
| Series |
Methods in molecular biology, 1064-3745 ; 350 |
|
Methods in molecular biology (Clifton, N.J.) ; v. 350
|
| Contents |
Infrared temperature-jump study of the folding dynamics of alpha-helices and beta-hairpins / F. Gai, D. Du and Y. Xu -- The use of high-pressure nuclear magnetic resonance to study protein folding / M.W. Lassalle and K. Akasaka -- Characterization of denatured proteins using residual dipolar couplings / E.B. Gebel and D. Shortle -- Characterizing residual structure in disordered protein States using nuclear magnetic resonance / D. Eliezer -- Population and structure determination of hidden folding intermediates by native-state hydrogen exchange-directed protein engineering and nuclear magnetic resonance / Y. Bai, H. Feng and Z. Zhou -- Characterizing protein folding transition States using Psi-analysis / A.D. Pandit [and others] -- Advances in the analysis of conformational transitions in peptides using differential scanning calorimetry / W.W. Streicher and G.I. Makhatadze -- Application of single molecule Forster resonance energy transfer to protein folding / B. Schuler -- Single molecule studies of protein folding using atomic force microscopy / S.P. Ng, L.G. Randles and J. Clarke -- Using triplet-triplet energy transfer to measure conformational dynamics in polypeptide chains / B. Fierz [and others] -- A hierarchical protein folding scheme based on the building block folding model / N. Haspel [and others] -- Replica exchange molecular dynamics method for protein folding simulation / R. Zhou -- Estimation of folding probabilities and phi values from molecular dynamics simulations of reversible Peptide folding / F. Rao, G. Settanni and A. Caflisch -- Packing regularities in biological structures relate to their dynamics / R.L. Jernigan and A. Kloczkowski -- Intermediates and transition states in protein folding / D. Thirumalai and D.K. Klimov -- Thinking the impossible: how to solve the protein folding problem with and without homologous structures and more / R. Casadio [and others] |
| Summary |
Protein Folding Protocols presents protocols for studying and characterizing protein folding from the unfolded to the folded state. Covering experiment and theory, bioinformatics approaches, and state-of-the-art simulation protocols for better sampling of the conformational space, this volume describes a broad range of techniques to study, predict, and analyze the protein folding process. Protein Folding Protocols also provides sample approaches toward the prediction of protein structure starting from the amino acid sequence, in the absence of overall homologous sequences. These approaches have tremendous implications, ranging from drug design, functional assignment, comprehension of the nature of regulation, understanding molecular machines, viral entry into cells, and putting together cellular pathways and their dynamics |
| Bibliography |
Includes bibliographical references and index |
| Notes |
Print version record |
| Subject |
Protein folding.
|
|
Proteins -- Conformation.
|
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Proteins -- Analysis.
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Protein Folding
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Protein Conformation
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Proteins -- analysis
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SCIENCE -- Life Sciences -- Biochemistry.
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Protein folding
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Proteins -- Analysis
|
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Proteins -- Conformation
|
| Genre/Form |
Laboratory manuals.
|
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Manuels de laboratoire.
|
| Form |
Electronic book
|
| Author |
Bai, Yawen.
|
|
Nussinov, Ruth.
|
| ISBN |
1588296229 |
|
1597451894 |
|
9781597451895 |
|
9781588296221 |
|
1280832584 |
|
9781280832581 |
|
