scholarly journals Disulfide bonds in protein folding studies: friends or foes?

1997 ◽  
Vol 44 (3) ◽  
pp. 433-452 ◽  
Author(s):  
M Dadlez
Keyword(s):  
Protein Folding ◽  
Disulfide Bonds ◽  
Model Systems ◽  
Bovine Pancreatic Trypsin Inhibitor ◽  
General Mechanism ◽  
Folding Pathway ◽  
Protein Model ◽  
Folding Pathways ◽  
Pancreatic Trypsin Inhibitor ◽  
Protein Folding Pathways

The studies on protein folding pathways utilizing disulfide bonds as reporter groups in several protein model systems are reviewed. Implications for a general mechanism of protein folding are discussed. An updated folding pathway for bovine pancreatic trypsin inhibitor (BPTI) based on recent data is proposed.

Disulphide-coupled protein folding pathways

1995 ◽  
Vol 348 (1323) ◽  
pp. 5-10 ◽  
Keyword(s):  
Protein Folding ◽  
Trypsin Inhibitor ◽  
Native Species ◽  
Molten Globule ◽  
Disulphide Bond ◽  
Bovine Pancreatic Trypsin Inhibitor ◽  
Disulphide Bond Formation ◽  
Folding Pathways ◽  
Pancreatic Trypsin Inhibitor ◽  
Protein Folding Pathways

Protein folding pathways that involve disulphide bond formation can be determined in great detail. Those of bovine pancreatic trypsin inhibitor, α-lactalbumin and ribonucleases A and T 1 are compared and contrasted. In each species, whatever conformation favours one disulphide bond over another is stabilized to the same extent by the presence of that disulphide bond in the disulphide intermediates. The pathways differ markedly in the nature of that conformation: in bovine pancreatic trypsin inhibitor a crucial intermediate is partly folded, in α-lactalbumin the intermediates tend to adopt to varying extents the molten globule conformation, while in the ribonucleases the early disulphide intermediates are largely unfolded, and none predominate. In each case, however, the slowest step is formation of a disulphide bond that will be buried in a stable folded conformation; the most rapid step is formation of an accessible disulphide bond on the surface of a folded conformation. Quasi-native species with the native conformation, but incomplete disulphide bonds, can either increase or decrease the rate of further disulphide formation.

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.

Self-consistent calculation of protein folding pathways

2017 ◽  
Vol 147 (6) ◽  
pp. 064108 ◽  
Author(s):  
S. Orioli ◽  
S. a Beccara ◽  
P. Faccioli
Keyword(s):  
Protein Folding ◽  
Consistent Calculation ◽  
Self Consistent ◽  
Folding Pathways ◽  
Protein Folding Pathways
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