Protein folding intermediates with rapidly exchangeable amide protons contain authentic hydrogen-bonded secondary structures

Biochemistry ◽  
1995 ◽  
Vol 34 (9) ◽  
pp. 2998-3008 ◽  
Author(s):  
J. Inaki Guijarro ◽  
Michael Jackson ◽  
Alain F. Chaffotte ◽  
Muriel Delepierre ◽  
Henry H. Mantsch ◽  
...  
Keyword(s):  
Protein Folding ◽  
Secondary Structures ◽  
Folding Intermediates ◽  
Amide Protons ◽  
Hydrogen Bonded

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.

Structure of Stable Protein Folding Intermediates by Equilibrium ϕ-Analysis: The Apoflavodoxin Thermal Intermediate

2004 ◽  
Vol 344 (1) ◽  
pp. 239-255 ◽  
Author(s):  
Luis A. Campos ◽  
Marta Bueno ◽  
Jon Lopez-Llano ◽  
María Ángeles Jiménez ◽  
Javier Sancho
Keyword(s):  
Protein Folding ◽  
Folding Intermediates

Protein folding intermediates and Alzheimer’s disease

2006 ◽  
pp. 319-321
Author(s):  
J. P. Lee ◽  
S- S. Zhang ◽  
C. Clish ◽  
N. Casey ◽  
D. Hassell ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Protein Folding ◽  
Folding Intermediates

Mimicking cotranslational folding of prosubtilisin E in vitro

2020 ◽  
Vol 167 (5) ◽  
pp. 473-482 ◽  
Author(s):  
Sung-Gun Kim ◽  
Yu-Jen Chen ◽  
Liliana Falzon ◽  
Jean Baum ◽  
Masayori Inouye
Keyword(s):  
Crucial Role ◽  
Tertiary Structure ◽  
Molten Globule ◽  
Secondary Structures ◽  
Terminal Region ◽  
Folding Intermediates ◽  
C Terminus ◽  
Cotranslational Folding ◽  
N Terminus

Abstract Nascent polypeptides are synthesized on ribosomes starting at the N-terminus and simultaneously begin to fold during translation. We constructed N-terminal fragments of prosubtilisin E containing an intramolecular chaperone (IMC) at N-terminus to mimic cotranslational folding intermediates of prosubtilisin. The IMC-fragments of prosubtilisin exhibited progressive enhancement of their secondary structures and thermostabilities with increasing polypeptide length. However, even the largest IMC-fragment with 72 residues truncated from the C-terminus behaved as a molten globule, indicating the requirement of the C-terminal region to have a stable tertiary structure. Furthermore, truncation of the IMC in the IMC-fragments resulted in aggregation, suggesting that the IMC plays a crucial role to prevent misfolding and aggregation of cotranslational folding intermediates during translation of prosubtilisin polypeptide.

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