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Protein flexibility and folding

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Published by Elsevier in Amsterdam, New York .
Written in English

Subjects:

  • Protein folding -- Congresses.,
  • Protein folding -- Computer simulation -- Congresses.

Book details:

Edition Notes

Other titlesJournal of molecular graphics & modelling (Online)
Statementedited by Leslie A. Kuhn and Michael F. Thorpe.
GenreCongresses.
SeriesBiological modeling series
ContributionsKuhn, Leslie A., Thorpe, M. F.
Classifications
LC ClassificationsQP551 .P695819 2001
The Physical Object
Pagination178 p. :
Number of Pages178
ID Numbers
Open LibraryOL3967463M
ISBN 100444508163
LC Control Number2001273443
OCLC/WorldCa47822888

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Local flexibility: atoms and residues. Portions of protein structures often deviate from the equilibrium state. Some such excursions are harmonic, such as stochastic fluctuations of chemical bonds and bond angles. Others are anharmonic, such as sidechains that jump between separate discrete energy minima, or rotamers. [citation needed]Evidence for local flexibility is often obtained from NMR. In Protein Structure, Stability, and Folding, Kenneth P. Murphy and a panel of internationally recognized investigators describe some of the newest experimental and theoretical methods for investigating these critical events and processes. Among the techniques discussed are the many methods for calculating aspects of protein stability and Price: $ Protein folding is the physical process by which a protein chain acquires its native 3-dimensional structure, a conformation that is usually biologically functional, in an expeditious and reproducible manner. It is the physical process by which a polypeptide folds into its characteristic and functional three-dimensional structure from a random coil. Each protein exists as an unfolded. A simple minimalistic off-lattice protein model is a beads-on-a-string model, representing a chain with maximal flexibility. One drawback of a beads-on-a-string model is that its chain flexibility is higher than that observed in real proteins, so, as a result, the protein model folding kinetics is often altered, due to the conformational.

Protein and Peptide Folding, Misfolding, and Non-Folding begins with an introduction that explains why research on IDPs has significantly expanded in the past few years. Next, the book is divided into three sections: Conformational Analysis of Unfolded States. Disordered Peptides and Molecular Recognition. Proteins are the most versatile macromolecules in living systems and serve crucial functions in essentially all biological processes. They function as catalysts, they transport and store other molecules such as oxygen, they provide mechanical support and immune protection, they generate movement, they transmit nerve impulses, and they control growth and by: The papers in this volume are from the workshop on Protein Flexibility and Folding held in Traverse City, Michigan from August 13 - 17, The purpose of the workshop was to bring together diverse people interested in protein folding and flexibility from theoretical, computational and experimental perspectives and to encourage discussion on new approaches and challenges in the field. The book systematically summarizes and presents the results of several decades of worldwide fundamental research on protein physics, structure, and folding, describing many physical models that help readers make estimates and predictions of physical processes that occur in proteins.

Understanding the way in which proper protein folding is controlled by the cell is required to find a cure for Alzheimer's and other diseases caused by misfolded proteins. This unique handbook contains the expertise from more than 60 research groups, covering the entire range of topics in protein folding - from biophysics to molecular medicine. The book gives a deep insight into the principles and concepts of the kinetic and structural resolution of fast chemical and biophysical reactions of proteins with emphasis on protein-folding reactions. The study of fast protein-folding reactions and the understanding of the folding paradox have significantly advanced due to the recent. Throughout the book, theoretical as well as practical aspects are addressed, including detailed protocols for key techniques in protein folding research. The comprehensiveness and outstanding quality of the carefully selected contributions render this the ultimate resource for every scientist with an Format: Hardcover. Protein Folding book. Read reviews from world’s largest community for readers. The phenomenon of protein folding has become the focus of intense scientif 4/5.