Structural analysis of lysine-4 methylated histone H3 proteins using synchrotron radiation circular dichroism spectroscopy

Chirality ◽  
2018 ◽  
Vol 30 (5) ◽  
pp. 536-540 ◽  
Author(s):  
Yudai Izumi ◽  
Koichi Matsuo ◽  
Hirofumi Namatame
Keyword(s):  
Circular Dichroism ◽  
Structural Analysis ◽  
Synchrotron Radiation ◽  
Histone H3 ◽  
Circular Dichroism Spectroscopy ◽  
Circular Dichroïsm

Synchrotron radiation circular dichroism spectroscopy applied to metmyoglobin and a 4-?-helix bundle carboprotein

Biopolymers ◽  
2005 ◽  
Vol 78 (1) ◽  
pp. 46-52 ◽  
Author(s):  
Peter W. Thulstrup ◽  
Jesper Brask ◽  
Knud J. Jensen ◽  
Erik Larsen
Keyword(s):  
Circular Dichroism ◽  
Synchrotron Radiation ◽  
Circular Dichroism Spectroscopy ◽  
Helix Bundle ◽  
Circular Dichroïsm

Synchrotron radiation circular dichroism (SRCD) spectroscopy: an enhanced method for examining protein conformations and protein interactions

2010 ◽  
Vol 38 (4) ◽  
pp. 861-873 ◽  
Author(s):  
B.A. Wallace ◽  
Robert W. Janes
Keyword(s):  
Circular Dichroism ◽  
Synchrotron Radiation ◽  
Protein Interactions ◽  
Structural Information ◽  
Data Bank ◽  
Cd Spectroscopy ◽  
Circular Dichroism Spectroscopy ◽  
Protein Conformations ◽  
Mutant Proteins ◽  
Circular Dichroïsm

CD (circular dichroism) spectroscopy is a well-established technique in structural biology. SRCD (synchrotron radiation circular dichroism) spectroscopy extends the utility and applications of conventional CD spectroscopy (using laboratory-based instruments) because the high flux of a synchrotron enables collection of data at lower wavelengths (resulting in higher information content), detection of spectra with higher signal-to-noise levels and measurements in the presence of absorbing components (buffers, salts, lipids and detergents). SRCD spectroscopy can provide important static and dynamic structural information on proteins in solution, including secondary structures of intact proteins and their domains, protein stability, the differences between wild-type and mutant proteins, the identification of natively disordered regions in proteins, and the dynamic processes of protein folding and membrane insertion and the kinetics of enzyme reactions. It has also been used to effectively study protein interactions, including protein–protein complex formation involving either induced-fit or rigid-body mechanisms, and protein–lipid complexes. A new web-based bioinformatics resource, the Protein Circular Dichroism Data Bank (PCDDB), has been created which enables archiving, access and analyses of CD and SRCD spectra and supporting metadata, now making this information publicly available. To summarize, the developing method of SRCD spectroscopy has the potential for playing an important role in new types of studies of protein conformations and their complexes.

scholarly journals Circular dichroism and synchrotron radiation circular dichroism spectroscopy: tools for drug discovery

2003 ◽  
Vol 31 (6) ◽  
pp. 1531-1531 ◽  
Author(s):  
B.A. WALLACE ◽  
ROBERT W. JANES
Keyword(s):  
Circular Dichroism ◽  
Drug Discovery ◽  
Synchrotron Radiation ◽  
Circular Dichroism Spectroscopy ◽  
Title Page ◽  
Online Journal ◽  
Circular Dichroïsm

On the title page of the article (p. 631), the first author's name was shown incorrectly as “Bonnie A. Wallace”; this should have been “B.A. Wallace”. This has been corrected for the online journal.

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