scholarly journals Unusual structural characteristics of theMycobacterium tuberculosispentapeptide repeat protein MfpA

2010 ◽  
Vol 24 (3-4) ◽  
pp. 339-341
Author(s):  
S. Khrapunov ◽  
H. Cheng ◽  
S. Hegde ◽  
J. Blanchard ◽  
M. Brenowitz
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Circular Dichroism ◽  
Drug Discovery ◽  
Solution Structure ◽  
Structural Characteristics ◽  
Circular Dichroism Spectroscopy ◽  
Repeat Protein ◽  
Oligomer Formation ◽  
Novel Target ◽  
Circular Dichroïsm

The solution structure and refolding of theMycobacterium tuberculosispentapeptide repeat protein MfpA was explored by fluorescence and circular dichroism spectroscopy. Our results show that MfpA exists in two stable structural forms which exclusively favor dimer or oligomer formation. The structural malleability of MfpA may provide a novel target for drug discovery.

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.

scholarly journals Conformation Transition Kinetics of Silk Fibroin in Aqueous Solution Explored Using Circular Dichroism Spectroscopy

2021 ◽  
Vol 6 (8) ◽  
pp. 1735-1740
Author(s):  
Sora Lee ◽  
Soo Hyun Kim ◽  
You‐Young Jo ◽  
Wan‐Taek Ju ◽  
Hyun‐Bok Kim ◽  
...  
Keyword(s):  
Aqueous Solution ◽  
Circular Dichroism ◽  
Silk Fibroin ◽  
Circular Dichroism Spectroscopy ◽  
Kinetics Of ◽  
Circular Dichroïsm ◽  
Conformation Transition

Enantiopure methoxetamine stereoisomers: chiral resolution, conformational analysis, UV-circular dichroism spectroscopy and electronic circular dichroism

2021 ◽  
Author(s):  
Kun Won Lee ◽  
Ahmed H. E. Hassan ◽  
Youngdo Jeong ◽  
Seolmin Yoon ◽  
Seung-Hwan Kim ◽  
...  
Keyword(s):  
Circular Dichroism ◽  
Conformational Analysis ◽  
Absolute Configuration ◽  
Circular Dichroism Spectroscopy ◽  
Chiral Resolution ◽  
Treatment Resistant Depression ◽  
Treatment Resistant ◽  
Electronic Circular Dichroism ◽  
Resistant Depression ◽  
Circular Dichroïsm

Enantioseparation and assignment of absolute configuration of methoxetamine (MXE) enantiopure stereoisomers; a promising novel antidepressant for management of treatment-resistant depression.

scholarly journals Circular dichroism spectroscopy of membrane proteins

2016 ◽  
Vol 45 (18) ◽  
pp. 4859-4872 ◽  
Author(s):  
A. J. Miles ◽  
B. A. Wallace
Keyword(s):  
Circular Dichroism ◽  
Membrane Proteins ◽  
Circular Dichroism Spectroscopy ◽  
Circular Dichroism Spectra ◽  
Helical Bundle ◽  
Beta Barrel ◽  
Circular Dichroïsm

Circular dichroism spectra of helical bundle (red), beta barrel (blue), and mixed helical/sheet/unordered (green) membrane proteins.

scholarly journals Detection of Protein-Protein Interactions in the Alkanesulfonate Monooxygenase System from Escherichia coli

2006 ◽  
Vol 188 (23) ◽  
pp. 8153-8159 ◽  
Author(s):  
Kholis Abdurachim ◽  
Holly R. Ellis
Keyword(s):  
Circular Dichroism ◽  
Protein Interactions ◽  
Visible Region ◽  
Circular Dichroism Spectroscopy ◽  
Flavin Mononucleotide ◽  
Stable Complex ◽  
Monooxygenase System ◽  
Protein Protein Interactions ◽  
Alkanesulfonate Monooxygenase ◽  
Circular Dichroïsm

ABSTRACT The two-component alkanesulfonate monooxygenase system utilizes reduced flavin as a substrate to catalyze a unique desulfonation reaction during times of sulfur starvation. The importance of protein-protein interactions in the mechanism of flavin transfer was analyzed in these studies. The results from affinity chromatography and cross-linking experiments support the formation of a stable complex between the flavin mononucleotide (FMN) reductase (SsuE) and monooxygenase (SsuD). Interactions between the two proteins do not lead to overall conformational changes in protein structure, as indicated by the results from circular dichroism spectroscopy in the far-UV region. However, subtle changes in the flavin environment of FMN-bound SsuE that occur in the presence of SsuD were identified by circular dichroism spectroscopy in the visible region. These data are supported by the results from fluorescent spectroscopy experiments, where a dissociation constant of 0.0022 ± 0.0010 μM was obtained for the binding of SsuE to SsuD. Based on these studies, the stoichiometry for protein-protein interactions is proposed to involve a 1:1 monomeric association of SsuE with SsuD.

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