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Protein Folding Protocols 1st Edition by Yawen Bai, Ruth Nussinov ISBN 1617376760 978-1617376764

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Protein Folding Protocols 1st Edition Feng Gai Digital Instant Download

Author(s): Feng Gai, Deguo Du, Yao Xu (auth.), Yawen Bai, Ruth Nussinov (eds.)
ISBN(s): 9781597451895, 1597451894
Edition: 1
File Details: PDF, 5.14 MB
Year: 2006
Language: english
SKU: EB-4287084 Category: Tags: , , , ,

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Product details:

ISBN 10:  1617376760

ISBN 13: 978-1617376764 

Author: Yawen Bai, Ruth Nussinov 

Protein Folding Protocols presents protocols for studying and characterizing steps and conformational ensembles populating pathways in protein folding from the unfolded to the folded state. It further presents a sample of approaches toward the prediction of protein structure starting from the amino acid sequence, in the absence of overall homologous sequences. Protein folding is a crucial step in the transfer of genetic information from the DNA to the protein. The Genome Project has led to a huge number of available DNA sequences and, therefore, protein sequences. The Structural Genomics initiative largely aims to obtain “new” folds not currently present in the Protein Data Bank. Yet, the number of available structures inevitably lags behind the number of sequences. At the same time, an equally important problem is to find out the types and scope of dissimilar (nonhomologous) protein sequences that adopt a similar fold. Assembling data and comprehension of the sequence space of protein folds should be very useful in computational protein structure prediction. This would enhance the scope of homology modeling, which currently is the method of choice. Thus, experimental and theoretical studies on the relationship between sequence and structure are critical. Figuring out the relationship between sequence and structure would further assist in the prediction of fibril structures observed in protein misfolding diseases, and in figuring out the conformational changes and dynamics resulting from mutations. Protein folding is one of the most important and challenging problems in current molecular and chemical biology.

Table of contents:

1: Infrared Temperature-Jump Study of the Folding Dynamics of α-Helices and β-Hairpins
2: The Use of High-Pressure Nuclear Magnetic Resonance to Study Protein Folding
3: Characterization of Denatured Proteins Using Residual Dipolar Couplings
4: Characterizing Residual Structure in Disordered Protein States Using Nuclear Magnetic Resonance
5: Population and Structure Determination of Hidden Folding Intermediates by Native-State Hydrogen Exchange-Directed Protein Engineering and Nuclear Magnetic Resonance
6: Characterizing Protein Folding Transition States Using Ψ-Analysis
7: Advances in the Analysis of Conformational Transitions in Peptides Using Differential Scanning Calorimetry
8: Application of Single Molecule Förster Resonance Energy Transfer to Protein Folding
9: Single Molecule Studies of Protein Folding Using Atomic Force Microscopy
10: Using Triplet-Triplet Energy Transfer to Measure Conformational Dynamics in Polypeptide Chains
11: A Hierarchical Protein Folding Scheme Based on the Building Block Folding Model
12: Replica Exchange Molecular Dynamics Method for Protein Folding Simulation
13: Estimation of Folding Probabilities and Φ Values From Molecular Dynamics Simulations of Reversible Peptide Folding
14: Packing Regularities in Biological Structures Relate to Their Dynamics
15: Intermediates and Transition States in Protein Folding
16: Thinking the Impossible

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Tags: Yawen Bai, Protein, Folding, Protocols