Instrumental Analysis of Intrinsically Disordered Proteins / Wiley Series in Protein and Peptide Science (PDF)

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.