عنوان

Statistical Mechanics, Protein Structure, and Protein Substrate Interactions

(Number (ISBN

9781489913494

(Number (ISBN

9781489913517

Number

b404807

Title Proper

Statistical Mechanics, Protein Structure, and Protein Substrate Interactions

General Material Designation

[Book]

First Statement of Responsibility

edited by Sebastian Doniach.

Place of Publication, Distribution, etc.

Boston, MA :

Name of Publisher, Distributor, etc.

Imprint: Springer,

Date of Publication, Distribution, etc.

1994.

Series Title

NATO ASI Series, Series B: Physics,

Volume Designation

325

ISSN of Series

0258-1221 ;

Text of Note

Protein Folding Intermediates -- Pathways and Mechanism of Protein Folding -- The Folding Pathway of Apomyoglobin -- Circular Dichroism Stopped-Flow Studies of Folding Intermediates -- Native-like Intermediates in Protein Folding -- A First-Order Phase Transition Between a Compact Denatured State and a Random Coil State in Staphylococcal Nuclease -- Studies in Protein Stability -- Studies on 'Hyperstable' Proteins: Crystallins from the Eye-Lens and Enzymes from Thermophilic Bacteria -- Origins of Mutation Induced Stability Changes in Barnase: An Analysis Based on Free Energy Calculations -- Basic Interactions -- Monte Carlo Simulation of Electrostatic Interactions in Biomolecules -- The Molecular Origin of the Large Entropies of Hydrophobic Hydration -- Statistical Mechanical Models and Protein States -- Statistical Mechanics of Secondary Structures in Proteins: Characterization of a Molten Globule-like State -- Hydrophobic Zippers: A Conformational Search Strategy for Proteins -- Theoretical Perspectives on In Vitro and In Vivo Protein Folding -- On the Configurations Accessible to Folded and to Denatured Proteins -- Exploring Conformation Space -- Experiences with Dihedral Angle Space Monte Carlo Search for Small Protein Structures -- Constrained Langevin Dynamics of Polypeptide Chains -- MOIL: A Molecular Dynamics Program with Emphasis on Conformational Searches and Reaction Path Calculations -- Flexibility in the Fc Region of Immunoglobulin G -- NMR Data and Protein Structure -- Computer-Supported Protein Structure Determination by NMR -- Enumeration with Constraints: A Possible Approach to Protein Structure Reconstruction from NMR Data -- A Decomposition of the nOe Intensity Matrix -- Membrane Proteins -- Structure and Dynamics of Membrane Proteins -- Steps Toward Predicting the Structure of Membrane Proteins -- The Protein Data Base: Fold Families and Structure Prediction -- Protein Fold Families and Structural Motifs -- Data Based Modeling of Proteins -- Applications of Knowledge Based Mean Fields in the Determination of Protein Structures -- A New Approach to Protein Folding Calculations -- Knowledge Based Potentials for Predicting the Three-Dimensional Conformation of Proteins -- Protein-Substrate Interactions -- Protein-Protein Recognition: An Analysis by Docking Simulation -- Molecular Dynamics Simulation of an Antigen-Antibody Complex: Hydration Structure and Dissociation Dynamics -- Multiple Conformations of Cystatin, Mung Bean Inhibitor and Serpins -- Structure and tRNA Phe-Binding Properties of the Zinc Finger Motifs of HIV-1 Nucleocapsid Protein -- Electrostatic Complementarity in Protein-Substrate Interactions and Ligand Design -- Molecular Engineering in the Preparation of Bioactive Peptides -- Author Index.

0

Text of Note

A number of factors have come together in the last couple of decades to define the emerging interdisciplinary field of structural molecular biology. First, there has been the considerable growth in our ability to obtain atomic-resolution structural data for biological molecules in general, and proteins in particular. This is a result of advances in technique, both in x-ray crystallography, driven by the development of electronic detectors and of synchrotron radiation x-ray sources, and by the development ofNMR techniques which allow for inference of a three-dimensional structure of a protein in solution. Second, there has been the enormous development of techniques in DNA engineering which makes it possible to isolate and clone specific molecules of interest in sufficient quantities to enable structural measurements. In addition, the ability to mutate a given amino acid sequence at will has led to a new branch of biochemistry in which quantitative measurements can be made assessing the influence of a given amino acid on the function of a biological molecule. A third factor, resulting from the exponential increase in computing power available to researchers, has been the emergence of a growing body of people who can take the structural data and use it to build atomic-scale models of biomolecules in order to try and simulate their motions in an aqueous environment, thus helping to provide answers to one of the most basic questions of molecular biology: the relation of structure to function.

International Standard Book Number

9781489913517

Title

Springer eBooks

Parallel Title

Proceedings of a NATO ARW held in Cargese, Corsica, France, June 1-5, 1993

Life sciences.

Physiology.

Doniach, Sebastian.

SpringerLink (Online service)

Date of Transaction

20190307162300.0

Electronic name

[Book]

Y