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Protein Folding
By Eric C. Walters (Edited by)

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Format
Hardback, 621 pages
Published
United States, 23 May 2011
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Proteins are an important class of biological macromolecules present in every biological organism. Proteins are synthesised on ribosomes as a linear chain of amino acid residues in a specific order from information encoded within the DNA. In order to function, each newly synthesised chain must fold into the unique 3-D structure that is characteristic of the individual protein. Protein folding is a highly specific process and each protein has a specific fold to perform its specific function. Uncovering the mechanisms through which such processes take place is one of the greatest challenges in the post genomic era. This book presents current research from around the globe in the study of protein folding, including heterologous protein folding in yeast; how homodimeric proteins fold and assemble; ribosome assisted protein folding; protein disulphide isomerases; and self-assembling peptids for biomedical applications.


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£240
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£349.99
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Product Description

Proteins are an important class of biological macromolecules present in every biological organism. Proteins are synthesised on ribosomes as a linear chain of amino acid residues in a specific order from information encoded within the DNA. In order to function, each newly synthesised chain must fold into the unique 3-D structure that is characteristic of the individual protein. Protein folding is a highly specific process and each protein has a specific fold to perform its specific function. Uncovering the mechanisms through which such processes take place is one of the greatest challenges in the post genomic era. This book presents current research from around the globe in the study of protein folding, including heterologous protein folding in yeast; how homodimeric proteins fold and assemble; ribosome assisted protein folding; protein disulphide isomerases; and self-assembling peptids for biomedical applications.

Product Details
EAN
9781617289903
ISBN
1617289906
Other Information
graphs, illus, diagrams
Dimensions
26.5 x 19.2 x 4 centimeters (1.31 kg)

Table of Contents

Preface; Protein Disulphide Isomerases: Diversity & Roles in Plants; Self-Assembling Peptides for Biomedical Applications: IR & Raman Spectroscopies for the Study of Secondary Structure; Stability & Stabilization of Proteins: The Ribonuclease A Example; Heterologous Protein Folding in Yeast; Modelling of Protein Folding & Prediction of Rate Based on Nucleation Mechanism; Intrinsically Unordered Proteins: Structural Properties, Prediction & Relevance; How Homodimeric Proteins Fold & Assembly?; The Relationship between Human MAT1A Mutations & Disease: A Folding & Association Problem?; Differential Scanning Calorimetry: Thermodynamic Analysis of the Unfolding Transitions of Proteins, Domains & Peptidic Fragments by Using Equilibrium Models; Study of Folding/Unfolding Kinetics of Lattice Proteins by Applying a Simple Statistical Mechanical Model for Protein Folding; Ribosome Assisted Protein Folding: Some of its Biological Implications; Index.

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