Kinetics of cis-trans isomerization and reductive elimination in dihydridobis(trimethylphosphine)platinum(II)

1988 ◽  
Vol 27 (10) ◽  
pp. 1768-1775 ◽  
Author(s):  
Diane L. Packett ◽  
William C. Trogler
1989 ◽  
Vol 11 (3) ◽  
pp. 179-189 ◽  
Author(s):  
Bruno Marcandalli ◽  
Pier Luigi Beltrame ◽  
Ernestina Dubini-Paglia ◽  
Alberto Seves

1932 ◽  
Vol 54 (6) ◽  
pp. 2208-2215 ◽  
Author(s):  
M. Nelles ◽  
G. B. Kistiakowsky

2019 ◽  
Vol 21 (1) ◽  
pp. 125
Author(s):  
Francesca Troilo ◽  
Francesca Malagrinò ◽  
Lorenzo Visconti ◽  
Angelo Toto ◽  
Stefano Gianni

SH2 domains are protein domains that modulate protein–protein interactions through a specific interaction with sequences containing phosphorylated tyrosines. In this work, we analyze the folding pathway of the C-terminal SH2 domain of the p85 regulatory subunit of the protein PI3K, which presents a proline residue in a cis configuration in the loop between the βE and βF strands. By employing single and double jump folding and unfolding experiments, we demonstrate the presence of an on-pathway intermediate that transiently accumulates during (un)folding. By comparing the kinetics of folding of the wild-type protein to that of a site-directed variant of C-SH2 in which the proline was replaced with an alanine, we demonstrate that this intermediate is dictated by the peptidyl prolyl cis-trans isomerization. The results are discussed in the light of previous work on the effect of peptidyl prolyl cis-trans isomerization on folding events.


1935 ◽  
Vol 57 (2) ◽  
pp. 269-271 ◽  
Author(s):  
G. B. Kistiakowsky ◽  
Walter R. Smith

1965 ◽  
Vol 69 (5) ◽  
pp. 1584-1587 ◽  
Author(s):  
G. Wettermark ◽  
J. Weinstein ◽  
J. Sousa ◽  
L. Dogliotti

2007 ◽  
Vol 208 (24) ◽  
pp. 2600-2610 ◽  
Author(s):  
Nicolae Hurduc ◽  
Dominique Adès ◽  
Joël Belleney ◽  
Alain Siove ◽  
Georges Sauvet

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