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Peptide Folding, Misfolding, and Nonfolding: Wiley Series in Protein and Peptide Science

Autor R Schweitzer–Sten
en Limba Engleză Hardback – 9 apr 2012
This book provides an overview on what researchers have learned about unfolded peptides and how this knowledge facilitates the understanding of (a) the folding process, (b) the binding of ligands to receptor molecules, and (c) peptide self-aggregation. In this context, different experimental, theoretical, and computational concepts and approaches are introduced. This book can become a very useful addition for graduate-level courses on protein folding for the education of undergraduate and graduate students in research groups, which are exploring peptide self-aggregation for biomedical and biotechnological purposes.
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Specificații

ISBN-13: 9780470591697
ISBN-10: 0470591692
Pagini: 576
Dimensiuni: 162 x 239 x 36 mm
Greutate: 0.98 kg
Editura: Wiley
Seria Wiley Series in Protein and Peptide Science

Locul publicării:Hoboken, United States

Public țintă

Researchers and students in biophysics, protein science, biochemistry, medical biochemistry, biotechnology and biomedical engineering, proteomics, structural biologists, protein folding experts, pharmacologists and drug discovery experts, molecular and cell biologists.

Cuprins


Notă biografică

Reinhard Schweitzer-Stenner, PhD, is Professor and currently the Head of the Chemistry Department at Drexel University. Dr. Schweitzer-Stenner also heads the biospectroscopy research group. His research investigates peptide structure and functionally relevant heme distortions as well as ligand-receptor binding on the surface of mast cells. With more than 150 published research articles, Dr. Schweitzer-Stenner is widely recognized as a leader and pioneer in the study of the conformational properties of unfolded peptides.

Descriere

This book provides an overview on what researchers have learned about unfolded peptides and how this knowledge facilitates the understanding of (a) the folding process, (b) the binding of ligands to receptor molecules, and (c) peptide self-aggregation.