On the role of chemical detail in simulating protein folding kinetics

2006 ◽  
Vol 323 (1) ◽  
pp. 66-77 ◽  
Author(s):  
Young Min Rhee ◽  
Vijay S. Pande
2006 ◽  
Vol 15 (3) ◽  
pp. 564-582 ◽  
Author(s):  
Paul A. Ellison ◽  
Silvia Cavagnero

Structure ◽  
2004 ◽  
Vol 12 (10) ◽  
pp. 1833-1845 ◽  
Author(s):  
Suhail A. Islam ◽  
Martin Karplus ◽  
David L. Weaver

2013 ◽  
Vol 4 (6) ◽  
pp. 597-604 ◽  
Author(s):  
Yuji Hidaka ◽  
Shigeru Shimamoto

AbstractDisulfide-containing proteins are ideal models for studies of protein folding as the folding intermediates can be observed, trapped, and separated by HPLC during the folding reaction. However, regulating or analyzing the structures of folding intermediates of peptides and proteins continues to be a difficult problem. Recently, the development of several techniques in peptide chemistry and biotechnology has resulted in the availability of some powerful tools for studying protein folding in the context of the structural analysis of native, mutant proteins, and folding intermediates. In this review, recent developments in the field of disulfide-coupled peptide and protein folding are discussed, from the viewpoint of chemical and biotechnological methods, such as analytical methods for the detection of disulfide pairings, chemical methods for disulfide bond formation between the defined Cys residues, and applications of diselenide bonds for the regulation of disulfide-coupled peptide and protein folding.


1993 ◽  
Vol 90 (5) ◽  
pp. 1942-1946 ◽  
Author(s):  
K. A. Dill ◽  
K. M. Fiebig ◽  
H. S. Chan

2016 ◽  
Vol 44 (22) ◽  
pp. 10898-10911 ◽  
Author(s):  
Guilhem Faure ◽  
Aleksey Y. Ogurtsov ◽  
Svetlana A. Shabalina ◽  
Eugene V. Koonin

2018 ◽  
Vol 114 (3) ◽  
pp. 414a
Author(s):  
Rayna M. Addabbo ◽  
Matthew D. Dalphin ◽  
Yue Liu ◽  
Miranda F. Mecha ◽  
Silvia Cavagnero

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