Supramolecular tryptophan-zipper forms a tripeptide as a regular proton transporter

CrystEngComm ◽  
2016 ◽  
Vol 18 (22) ◽  
pp. 4109-4114 ◽  
Author(s):  
Debasish Podder ◽  
Supriya Sasmal ◽  
Krishnendu Maji ◽  
Debasish Haldar
Keyword(s):  
2009 ◽  
Vol 15 (8) ◽  
pp. 523-532 ◽  
Author(s):  
Zihao Cheng ◽  
Robert E. Campbell

2012 ◽  
Vol 27 ◽  
pp. 557-564 ◽  
Author(s):  
Alexander Popp ◽  
Ling Wu ◽  
Timothy A. Keiderling ◽  
Karin Hauser

Folding dynamics forβ-structure loss and disordered structure gain were studied in a modelβ-hairpin peptide based on Cochran’s tryptophan zipper peptide Trpzip2, but with an altered Thr-Gly (TG) turn sequence, that is, SWTWETGKWTWK, using laser-induced temperature-jump (T-jump) kinetics with IR detection. As has been shown previously, the TG turn sequence reduces the thermodynamicβ-hairpin stability as compared to the Asn-Gly sequence used in Trpzip2 (TZ2-NG). In this study, we found that the TG-turn slows down the overall relaxation dynamics as compared to TZ2-NG, which were studied at higher temperatures where the time constants show little difference between relaxation of theβ-strand and the disordered conformation. These time constants become equivalent at lower temperatures for TZ2-TG than was seen for TZ2-NG. The correlation of thermodynamic stability and rates of relaxation suggests that the change from NG to TG turn results in a slowing of folding, lowerkf, with less change of the unfolding rate,ku, assuming two state behavior at higher temperatures.


Biochemistry ◽  
2006 ◽  
Vol 45 (28) ◽  
pp. 8579-8589 ◽  
Author(s):  
Schroeder M. Noble ◽  
Virginia E. Carnahan ◽  
Linda B. Moore ◽  
Tom Luntz ◽  
Hongbing Wang ◽  
...  
Keyword(s):  

2004 ◽  
Vol 101 (46) ◽  
pp. 16156-16161 ◽  
Author(s):  
J. Liu ◽  
W. Yong ◽  
Y. Deng ◽  
N. R. Kallenbach ◽  
M. Lu

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