Protein folding protocols /edited by Yawen Bai and Ruth Nussinov. --Humana Press,2006. –(58.17/M592/v.350)

Contents

Contents:

1.       Infrared temperature-jump study of the folding dynamics of α-Helices and β-Hairpins  1

2.       The Use of High-Pressure nuclear magnetic resonance to study protein folding  21

3.       Characterization of denatured proteins using residual dipolar couplings  39

4.       Characterizing residual structure in disordered proteins states using nuclear magnetic resonance  49

5.       Population and structure determination of hidden folding intermediates by native-state hydrogen exchange-directed protein engineering and nuclear magnetic resonance  69

6.       Characterizing protein folding transition states using ψ-Analysis  83

7.       Advances in the analysis of Conformational transitions in peptides using differential scaning calorimetry  105

8.       Application of single molecule forster resonance energy transfer to protein folding  115

9.       Single molecule studies of protein folding using atomic force microscopy  139

10.   Using triplet-triplet energy transfer to measure conformational dynamics in polypeptide chains  169

11.   A hierarchical protein folding scheme based on the building block folding mode  189

12.   Replica exchange molecular dynamics method for protein folding simulation  205

13.   Estimation of folding probabilityies and φ values from molecular for protein folding simulation  205

14.   Packing regularityes in biological structures relate to their dynamics  251

15.   Intermediates and transition states in protein folding  277

16.   Thinking the impossible: how to solve the protein folding problem with and without homologous structures and more  305