
Protein Folds. A Distance Based Approach
A Distance-Based Approach
CRC Press
1st Edition
Published on 20. October 1995
Book
Hardback
340 pages
978-0-8493-4009-3 (ISBN)
Description
Written by outstanding scientists in physics and molecular biology, this book addresses the most recent advances in the analysis of the protein folding processes and protein structure determination. Emphasis is also placed on modelling and presentation of experimental results of structural membrane bound proteins.
Many color plates help to illustrate structural aspects covered including:
Defining folds of protein domains
Structure determination from sequence
Distance geometry
Lattice theories
Membrane proteins
Protein-Ligand interaction
Topological considerations
Docking onto receptors
All analysis is presented with proven theory and experimentation.
Protein Folds: A Distance-Based Approach is an excellent text/reference for biotechnologists and biochemists as well as graduate students studying in the research sciences.
Many color plates help to illustrate structural aspects covered including:
Defining folds of protein domains
Structure determination from sequence
Distance geometry
Lattice theories
Membrane proteins
Protein-Ligand interaction
Topological considerations
Docking onto receptors
All analysis is presented with proven theory and experimentation.
Protein Folds: A Distance-Based Approach is an excellent text/reference for biotechnologists and biochemists as well as graduate students studying in the research sciences.
More details
Language
English
Place of publication
Bosa Roca
United States
Publishing group
Taylor & Francis Inc
Target group
College/higher education
Professional and scholarly
Professional
Dimensions
Height: 254 mm
Width: 178 mm
Weight
910 gr
ISBN-13
978-0-8493-4009-3 (9780849340093)
Schweitzer Classification
Persons
Bohr\, Henrik; Brunak\, Soren
Content
. Introduction. Overview. Three Paradoxes of Protein Folding. Protein-Ligand Complexes and Protein Biosynthesis. Conserved Water Molecules and Protein Folding in Fungal Peroxidases. Interplay between Metal Coordination Geometry and Protein Structure. Elongation Factor Tu: A G-Protein in Protein Biosynthesis. Electron Transfer of the Di-Heme Protein: Pseudomonas stutzeri cytochrome c4,. Profile Methods for Protein Structure and Fold Determination. Sequence Matching in Homology Modelling. Screening Genome Sequences for Known Folds. Protein Fold Determination Using a Small Number of Distance Restraints. How Many Protein Fold Classes Are To Be Found? Distance-Based Protein Structure Prediction and Evaluation. The Effect of a Distance-Cutoff on the Performance of The Distance Matrix Error When Used as a Potential Function to Drive Conformational Search. Protein Structure Prediction: How Can Self-Misleading Be Avoided? Sequence Space Analysis: Identification of Functionally or Structurally Important Residues in Protein Sequence Families. Fitting 1-D Predictions into 3-D Structures. Determination of Membrane Bound Protein Structure and Function. Modelling a-helical Integral Membrane Proteins. Use of Small Organic Compounds and Metal-ions as Structural and Functional Probes in 7TM Receptors. Using Sequence Information and Model Building to Explore Subtype Specificity in GPCRs. Statistical Mechanics and Kinetics of Protein Folding Processes. Proposed Rules of the Protein Folding Game. Protein Folding Studied by Monte Carlo Simulations. Folding Kinetics of Protein Like Heteropolymers. Energy Landscape and Folding Mechanisms in Proteins. Topological Aspects of Protein Folds. Resonator Driven Protein Folding: The Implication of Topology for Protein Structure and Folding. Chirality in Protein Structure. Packing within and between Subunits Defined by Internal Cavities. Protein Modelling and Docking. Modelling and Predicting a-helical Transmembrane Structures. HIV GP120 Docking Interactions and Inhibitor Design Based on an Atomic Structure Derived by Molecular Modelling Using the DREIDING II Force Field. A Model of the 3D Structure of Obelin-The Photoprotein From Obelia longissima. Index.
OTIs
7822, 2511, 4781
OTIs
7822, 2511, 4781