Circular dichroism and resonance Raman studies of cytochrome b562 from Escherichia coli

Biochemistry ◽  
1978 ◽  
Vol 17 (15) ◽  
pp. 3084-3091 ◽  
Author(s):  
Peter A. Bullock ◽  
Yash P. Myer
Keyword(s):  
Escherichia Coli ◽  
Circular Dichroism ◽  
Resonance Raman ◽  
Cytochrome B562 ◽  
Circular Dichroïsm

scholarly journals Circular dichroism investigation of Escherichia coli adenylate kinase.

1987 ◽  
Vol 262 (6) ◽  
pp. 2502-2506
Author(s):  
M. Monnot ◽  
A.M. Gilles ◽  
I.S. Girons ◽  
S. Michelson ◽  
O. Bârzu ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Circular Dichroism ◽  
Adenylate Kinase ◽  
Circular Dichroïsm

Folding Pathway of Escherichia coli Ribonuclease HI: A Circular Dichroism, Fluorescence, and NMR Study

Biochemistry ◽  
1995 ◽  
Vol 34 (51) ◽  
pp. 16552-16562 ◽  
Author(s):  
Kazuhiko Yamasaki ◽  
Kyoko Ogasahara ◽  
Katsuhide Yutani ◽  
Motohisa Oobatake ◽  
Shigenori Kanaya
Keyword(s):  
Escherichia Coli ◽  
Circular Dichroism ◽  
Folding Pathway ◽  
Nmr Study ◽  
Circular Dichroïsm

Circular dichroism and resonance Raman comparative studies of wild type cytochromec and F82H mutant

Biopolymers ◽  
2000 ◽  
Vol 57 (2) ◽  
pp. 77-84 ◽  
Author(s):  
Junwei Zheng ◽  
Shuyu Ye ◽  
Tianhong Lu ◽  
Therese M. Cotton ◽  
George Chumanov
Keyword(s):  
Circular Dichroism ◽  
Comparative Studies ◽  
Resonance Raman ◽  
Wild Type ◽  
Circular Dichroïsm

Physical studies on the ribosomal "A" protein from two archaebacteria, Halobacterium cutirubrum and Methanobacterium thermoautotrophicum

1984 ◽  
Vol 62 (1) ◽  
pp. 44-48 ◽  
Author(s):  
A. T. Gudkov ◽  
S. Yu Venyaminov ◽  
A. T. Matheson
Keyword(s):  
Escherichia Coli ◽  
Circular Dichroism ◽  
Secondary Structure ◽  
Quaternary Structure ◽  
Methanobacterium Thermoautotrophicum ◽  
Sedimentation Equilibrium ◽  
Effect Of Temperature ◽  
Extreme Halophile ◽  
Moderate Halophile ◽  
Circular Dichroïsm

Physical studies on the effect of temperature and ionic conditions on the secondary, tertiary, and quaternary structure of the ribosomal "A" protein, equivalent to L7/L12 in Escherichia coli, from two archaebacteria were performed using circular dichroism and sedimentation equilibrium measurements. The two archaebacteria investigated were Halobacterium cutirubrum, an extreme halophile, and Methanobacterium thermoautotrophicum, a thermophile which also showed properties of a moderate halophile. The changes in the secondary structure and the thermostability of these proteins were directly related to the internal salt concentrations of the two archaebacteria. At the higher salt concentrations the changes in the secondary structure resulted in changes in the tertiary and quaternary structure of these proteins.

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