Instrumental Analysis of Intrinsically Disordered Proteins

Instrumental techniques for analyzing intrinsically disordered proteins

The recently recognized phenomenon of protein intrinsic disorder is gaining significant interest among researchers, especially as the number of proteins and protein domains that have been shown to be intrinsically disordered rapidly grows. The first reference to tackle this little-documented area, Instrumental Analysis of Intrinsically Disordered Proteins: Assessing Structure and Conformation provides researchers with a much-needed, comprehensive summary of recent achievements in the methods for structural characterization of intrinsically disordered proteins (IDPs).

Chapters discuss:

• Assessment of IDPs in the living cell
• Spectroscopic techniques for the analysis of IDPs, including NMR and EPR spectroscopies, FTIR, circular dichroism, fluorescence spectroscopy, vibrational methods, and single-molecule analysis
• Single-molecule techniques applied to the study of IDPs
• Assessment of IDP size and shape
• Tools for the analysis of IDP conformational stability
• Mass spectrometry
• Approaches for expression and purification of IDPs

With contributions from an international selection of leading researchers, Instrumental Analysis of Intrinsically Disordered Proteins: Assessing Structure and Conformation fills an important need in a rapidly growing field. It is required reading for biochemists, biophysicists, molecular biologists, geneticists, cell biologists, physiologists, and specialists in drug design and development, proteomics, and molecular medicine with an interest in proteins and peptides.

Vladimir N. Uversky, PhD, is a Senior Research Professor at the Indiana University School of Medicine. He obtained his academic degrees from Moscow Institute of Physics and Technology (PhD) and the Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences. Professor Uversky has authored over 300 scientific publications and edited several books and book series on protein structure, function, folding, and misfolding. He is also an editor of several scientific journals.

Sonia Longhi, PhD, is a Director of Research at the Center for the National Scientific Research (CNRS), heading the Structural Disorder and Molecular Recognition group within the AFMB laboratory. She obtained her PhD from the Università degli Studi of Milan in 1993. She has authored more than sixty scientific publications and edited a book on measles virus nucleoprotein.