Intrinsically Disordered Proteins

2014
ISBN: 978-3-319-08920-1
Verlag: Springer International Publishing

Buch, Englisch, 61 Seiten, Format (B × H): 155 mm x 235 mm, Gewicht: 1358 g

Reihe: Protein Folding and Structure

In this brief, Vladimir Uversky discusses the paradigm-shifting phenomenon of intrinsically disordered proteins (IDPs) and hybrid proteins containing ordered domains and functional IDP regions (IDPRs). Beginning with an introduction to the concept of protein intrinsic disorder, Uversky then goes on to describe the peculiar amino acid sequences of IDPs, their structural heterogeneity, typical functions and disorder-based binding modes. In the final sections, Uversky discusses IDPs in human diseases and as potential drug targets. This volume provides a snapshot to researchers entering the field as well as providing a current overview for more experienced scientists in related areas.

Zielgruppe

Research

Autoren/Hrsg.

Uversky, Vladimir N.

Fachgebiete

• Naturwissenschaften Biowissenschaften Molekularbiologie
• Naturwissenschaften Biowissenschaften Proteinforschung

Inhaltsverzeichnis

Introducing the phenomenon of protein intrinsic disorder.- Peculiar amino acid sequences of soluble IDPs.- Natural abundance of IDPs/IDPRs.- Wavy evolution of intrinsic disorder: Reinventing the wheel.- Structural heterogeneity of IDPs: When almost everything is possible.- Typical functions of IDPs and IDPRs.- Binding promiscuity and multitude of the disorder-based binding modes.- IDPs/IDPRs in human diseases.- IDPs as potential drug targets.- Concluding remarks: Intrinsic disorder as a universal tool for solving protein mysteries and riddles.

Über Autor(innen)

Vladimir Uversky obtained his Ph.D. in biophysics from Moscow Institute of Physics and Technology (1991) and D.Sc. in biophysics from Institute of Experimental and Theoretical Biophysics, Russian Academy of Sciences (1998). He spent early career working on protein folding at Institute of Protein Research and the Institute for Biological Instrumentation (Russian Academy of Sciences). In 1998, he moved to the University of California Santa Cruz to work on protein folding, misfolding and protein intrinsic disorder. In 2004, he moved to the Center for Computational Biology and Bioinformatics at the Indiana University Purdue University Indianapolis to work on the intrinsically disordered proteins. Since 2010, he is with the Department of Molecular Biology at the University of South Florida.