Structural properties of arrestin studied by chemical modification and circular dichroism

Biochemistry ◽  
1992 ◽  
Vol 31 (16) ◽  
pp. 3902-3906 ◽  
Author(s):  
Krzysztof Palczewski ◽  
Jeannine H. Riazance-Lawrence ◽  
W. Curtis Johnson
Keyword(s):  
Circular Dichroism ◽  
Chemical Modification ◽  
Structural Properties ◽  
Circular Dichroïsm

scholarly journals A Raman, SERS and UV-circular dichroism spectroscopic study of N-acetyl-l-cysteine in aqueous solutions

2019 ◽  
Vol 43 (38) ◽  
pp. 15201-15212 ◽  
Author(s):  
R. A. Cobos Picot ◽  
M. Puiatti ◽  
A. Ben Altabef ◽  
R. J. G. Rubira ◽  
S. Sanchez-Cortes ◽  
...  
Keyword(s):  
Molecular Structure ◽  
Circular Dichroism ◽  
Aqueous Solutions ◽  
Spectroscopic Study ◽  
Electronic Properties ◽  
Structural Properties ◽  
Amine Groups ◽  
Circular Dichroïsm

The aim of this work is to evaluate the vibrational and structural properties of N-acetyl-l-cysteine (NAC), and its molecular structure and electronic properties in relation to the action of thiol and amine groups at different pH.

scholarly journals Biological Activities and Structural Properties of the Atypical Bacteriocins Mesenterocin 52B and Leucocin B-TA33a

2001 ◽  
Vol 67 (4) ◽  
pp. 1418-1422 ◽  
Author(s):  
C. Corbier ◽  
F. Krier ◽  
G. Mulliert ◽  
B. Vitoux ◽  
A.-M. Revol-Junelles
Keyword(s):  
Circular Dichroism ◽  
Structural Properties ◽  
Sequence Homology ◽  
Synthetic Peptides ◽  
Biological Activities ◽  
Modes Of Action ◽  
Amphiphilic Helix ◽  
High Sequence Homology ◽  
Circular Dichroïsm

ABSTRACT The antibacterial spectra and modes of action of synthetic peptides corresponding to mesenterocin 52B and leucocin B-TA33a greatly differ despite their high sequence homology. Circular dichroism experiments establish the capacity of each of these two peptides to partly fold into an amphiphilic helix that might be crucial for their adsorption at lipophilic-hydrophilic interfaces.

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