The role of cotranslation in protein folding: a lattice model study

Polymer ◽  
2004 ◽  
Vol 45 (2) ◽  
pp. 557-571 ◽  
Author(s):  
M.P. Morrissey ◽  
Z. Ahmed ◽  
E.I. Shakhnovich
Keyword(s):  
Protein Folding ◽  
Lattice Model ◽  
Model Study

scholarly journals Designability, thermodynamic stability, and dynamics in protein folding: A lattice model study

1999 ◽  
Vol 110 (2) ◽  
pp. 1252-1262 ◽  
Author(s):  
Régis Mélin ◽  
Hao Li ◽  
Ned S. Wingreen ◽  
Chao Tang
Keyword(s):  
Protein Folding ◽  
Thermodynamic Stability ◽  
Lattice Model ◽  
Model Study

A Lattice Model Study of α→β Transitions in Protein Folding

2000 ◽  
Vol 138 ◽  
pp. 406-407 ◽  
Author(s):  
George Chikenji ◽  
Macoto Kikuchi
Keyword(s):  
Protein Folding ◽  
Lattice Model ◽  
Model Study

Folding of peptides and proteins: role of disulfide bonds, recent developments

2013 ◽  
Vol 4 (6) ◽  
pp. 597-604 ◽  
Author(s):  
Yuji Hidaka ◽  
Shigeru Shimamoto
Keyword(s):  
Protein Folding ◽  
Disulfide Bonds ◽  
Bond Formation ◽  
Difficult Problem ◽  
Chemical Methods ◽  
Mutant Proteins ◽  
Folding Intermediates ◽  
Peptide Chemistry ◽  
Recent Developments

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.

scholarly journals Role of mRNA structure in the control of protein folding

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