Protein Folding in Silico, 1st Edition

Protein Folding Versus Protein Structure Prediction

 
Protein Folding in Silico, 1st Edition,I Roterman-Konieczna,ISBN9781907568176
 
 
 

I Roterman-Konieczna   

Woodhead Publishing

9781907568176

9781908818256

240

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Key Features

  • Discusses a range of ab initio models for protein structure prediction
  • Introduces a unique model based on experimental observations
  • Describes various methods for the quantitative assessment of the presented models from the viewpoint of information theory

Description

Protein folding is a process by which a protein structure assumes its functional shape of conformation, and has been the subject of research since the publication of the first software tool for protein structure prediction. Protein folding in silico approaches this issue by introducing an ab initio model that attempts to simulate as far as possible the folding process as it takes place in vivo, and attempts to construct a mechanistic model on the basis of the predictions made. The opening chapters discuss the early stage intermediate and late stage intermediate models, followed by a discussion of structural information that affects the interpretation of the folding process. The second half of the book covers a variety of topics including ligand binding site recognition, the "fuzzy oil drop" model and its use in simulation of the polypeptide chain, and misfolded proteins. The book ends with an overview of a number of other ab initio methods for protein structure predictions and some concluding remarks.

I Roterman-Konieczna

Dr Irena Roterman-Konieczna heads the bioinformatics group at the Jagiellonian University Medical College and the Faculty of Physics, Astronomy and Applied Computer Science. Her background is in theoretical chemistry, and her research focuses on bioinformatics, with specific focus on protein structure prediction.

Affiliations and Expertise

Jagiellonian University Medical College

Protein Folding in Silico, 1st Edition

The early-stage intermediate; The late-stage intermediate; Structural information involved in the interpretation of the stepwise protein folding process; The divergence entropy characterizing the internal force field in proteins; Ligand-binding-site recognition; Use of the “fuzzy oil drop” model to identify the complexation area in protein homodimers; Simulation of the polypeptide chain folding process using the “fuzzy oil drop” model; Misfolded proteins; A short description of other selected ab initio methods for protein structure prediction; Conclusion.
 
 
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