Facile Disulfide Bond Cleavage in Gaseous Peptide and Protein Cations by Ultraviolet Photodissociation at 157 nm

2005 ◽  
Vol 44 (39) ◽  
pp. 6399-6403 ◽  
Author(s):  
Y. M. Eva Fung ◽  
Frank Kjeldsen ◽  
Oleg A. Silivra ◽  
T. W. Dominic Chan ◽  
Roman A. Zubarev
Keyword(s):  
Disulfide Bond ◽  
Bond Cleavage ◽  
Ultraviolet Photodissociation

Facile Disulfide Bond Cleavage in Gaseous Peptide and Protein Cations by Ultraviolet Photodissociation at 157 nm

2005 ◽  
Vol 117 (39) ◽  
pp. 6557-6561 ◽  
Author(s):  
Y. M. Eva Fung ◽  
Frank Kjeldsen ◽  
Oleg A. Silivra ◽  
T. W. Dominic Chan ◽  
Roman A. Zubarev
Keyword(s):  
Disulfide Bond ◽  
Bond Cleavage ◽  
Ultraviolet Photodissociation

Alkali-modified soy proteins: Effect of salts and disulfide bond cleavage on adhesion and viscosity

1996 ◽  
Vol 73 (8) ◽  
pp. 1063-1066 ◽  
Author(s):  
U. Kalapathy ◽  
N. S. Hettiarachchy ◽  
D. Myers ◽  
K. C. Rhee
Keyword(s):  
Disulfide Bond ◽  
Bond Cleavage ◽  
Soy Proteins

Disulfide bond photochemistry: the effects of higher excited states and different molecular geometries on disulfide bond cleavage

2019 ◽  
Vol 21 (8) ◽  
pp. 4176-4183 ◽  
Author(s):  
Jun Cao ◽  
Dong-Chu Chen
Keyword(s):  
Excited State ◽  
Excited States ◽  
Disulfide Bond ◽  
Bond Cleavage ◽  
Trajectory Simulations ◽  
Higher Excited States

We have investigated the light-induced cleavage of disulfide bond using MS-CASPT2 based trajectory simulations and provided insights into the intrinsic excited state properties of disulfide molecules.

Cysteine-Selective Peptide Identification: Selenium-Based Chromophore for Selective S–Se Bond Cleavage with 266 nm Ultraviolet Photodissociation

2016 ◽  
Vol 88 (14) ◽  
pp. 7222-7229 ◽  
Author(s):  
W. Ryan Parker ◽  
Dustin D. Holden ◽  
Victoria C. Cotham ◽  
Hua Xu ◽  
Jennifer S. Brodbelt
Keyword(s):  
Bond Cleavage ◽  
Peptide Identification ◽  
Ultraviolet Photodissociation

Disulfide-Bond Cleavage and Formation in Proteins

Science ◽  
1965 ◽  
Vol 150 (3703) ◽  
pp. 1595-1598 ◽  
Author(s):  
O. Smithies
Keyword(s):  
Disulfide Bond ◽  
Bond Cleavage

Disulfide bond cleavage of human serum albumin and alterations of its secondary structure by cis-diamminedichloroplatinum(II)

1992 ◽  
Vol 85 (1-3) ◽  
pp. 39-44 ◽  
Author(s):  
Naoko Ohta ◽  
Toshihisa Yotsuyanagi ◽  
Danni Chen ◽  
Rikako Ono ◽  
Shigekazu Ito ◽  
...  
Keyword(s):  
Secondary Structure ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Disulfide Bond ◽  
Bond Cleavage

Effect of disulfide bond cleavage on the structure and conformation of glycinin

2009 ◽  
Vol 27 (4) ◽  
pp. 421-432 ◽  
Author(s):  
NAVIN KUMAR D. KELLA ◽  
WILLIAM E. BARBEAU ◽  
JOHN E. KINSELLA
Keyword(s):  
Disulfide Bond ◽  
Bond Cleavage

The Janus-faced role of external forces in mechanochemical disulfide bond cleavage

2013 ◽  
Vol 5 (8) ◽  
pp. 685-691 ◽  
Author(s):  
Przemyslaw Dopieralski ◽  
Jordi Ribas-Arino ◽  
Padmesh Anjukandi ◽  
Martin Krupicka ◽  
Janos Kiss ◽  
...  
Keyword(s):  
Disulfide Bond ◽  
Bond Cleavage ◽  
External Forces

Determination of —SH and —SS— groups in proteins. I. A reassessment of the use of methylmercuric iodide

1968 ◽  
Vol 46 (19) ◽  
pp. 3033-3040 ◽  
Author(s):  
W. F. Forbes ◽  
C. R. Hamlin
Keyword(s):  
Quantitative Determination ◽  
Disulfide Bond ◽  
Bond Cleavage ◽  
Reaction Times ◽  
High Reactivity ◽  
Insoluble Protein ◽  
Amperometric Titration ◽  
General Belief ◽  
Experimental Procedure

Amperometric titration with methylmercuric iodide was found to be unsatisfactory for the quantitative determination of —SH and —SS— values in several soluble proteins. It is concluded that the "high reactivity" of the mercurial has previously been overemphasized. Consistent values can, however, be obtained by permitting protein samples to react with an excess of the mercurial, for about 100 h, followed by the polarographic estimation of the remaining reagent. Contrary to general belief, this procedure was found to be more precise than amperometric titration, and, if appropriate precautions are taken, it is applicable to considerably smaller amounts (<0.5 μmole —SH or —SS—) of either soluble or insoluble protein. The necessary experimental procedure is described and results are reported for several proteins. For the compounds studied, methylmercuric iodide did not react at non-sulfhydryl sites, and did not additionally bind to the mercaptides formed; there was no indication of disulfide bond cleavage, despite the long reaction times used.

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