scholarly journals Novel Kinetic Intermediates Populated along the Folding Pathway of the Transmembrane β-Barrel OmpA

Biochemistry ◽  
2016 ◽  
Vol 56 (1) ◽  
pp. 47-60 ◽  
Author(s):  
Emily J. Danoff ◽  
Karen G. Fleming
Keyword(s):  
Folding Pathway ◽  
Kinetic Intermediates

scholarly journals Comparative Assessment of NMR Probes for the Experimental Description of Protein Folding Pathways with High-Pressure NMR

Biology ◽  
2021 ◽  
Vol 10 (7) ◽  
pp. 656
Author(s):  
Vincent Van Deuren ◽  
Yin-Shan Yang ◽  
Karine de Guillen ◽  
Cécile Dubois ◽  
Catherine Anne Royer ◽  
...  
Keyword(s):  
High Pressure ◽  
Staphylococcal Nuclease ◽  
Comparative Assessment ◽  
Side Chain ◽  
Folding Pathway ◽  
Hydrophobic Core ◽  
Folding Pathways ◽  
Partial Unfolding ◽  
Protein Folding Pathways ◽  
Similar Description

Multidimensional NMR intrinsically provides multiple probes that can be used for deciphering the folding pathways of proteins: NH amide and CH groups are strategically located on the backbone of the protein, while CH3 groups, on the side-chain of methylated residues, are involved in important stabilizing interactions in the hydrophobic core. Combined with high hydrostatic pressure, these observables provide a powerful tool to explore the conformational landscapes of proteins. In the present study, we made a comparative assessment of the NH, CH, and CH3 groups for analyzing the unfolding pathway of ∆+PHS Staphylococcal Nuclease. These probes yield a similar description of the folding pathway, with virtually identical thermodynamic parameters for the unfolding reaction, despite some notable differences. Thus, if partial unfolding begins at identical pressure for these observables (especially in the case of backbone probes) and concerns similar regions of the molecule, the residues involved in contact losses are not necessarily the same. In addition, an unexpected slight shift toward higher pressure was observed in the sequence of the scenario of unfolding with CH when compared to amide groups.

scholarly journals The disulfide folding pathway of potato carboxypeptidase inhibitor.

1994 ◽  
Vol 269 (35) ◽  
pp. 22087-22094
Author(s):  
J.Y. Chang ◽  
F. Canals ◽  
P. Schindler ◽  
E. Querol ◽  
F.X. Avilés
Keyword(s):  
Folding Pathway ◽  
Carboxypeptidase Inhibitor
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