scholarly journals Parallel folding pathway of proline-free staphylococcal nuclease studied by the stopped-flow double-jump method

2003 ◽  
Vol 17 (2-3) ◽  
pp. 203-212 ◽  
Author(s):  
Kiyoto Kamagata ◽  
Kunihiro Kuwajima
Keyword(s):  
Staphylococcal Nuclease ◽  
Folding Pathway ◽  
Stopped Flow ◽  
Native State ◽  
Flow Method ◽  
Folding Mechanism ◽  
Parallel Pathways ◽  
Parallel Folding ◽  
Refolding Kinetics

The folding mechanism of proline‒free staphylococcal nuclease (SNase (pro−)) (P11A, P31A, P42A, P47T, P56A, P117G) was investigated using the double‒jump stopped‒flow method (interrupted refolding). This method has enabled us to specifically monitor the amount of the native molecules during the refolding. The results indicate that the middle and slow phases observed in the refolding kinetics represent the formation of the native state (IM→N, IS→N) and that the folding mechanism of SNase (pro−) is not represented by a single sequential pathway, but at least two parallel pathways are required for interpreting the results.

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.

Combined electrolysis—stopped flow method (SFEL)

1991 ◽  
Vol 302 (1-2) ◽  
pp. 285-291 ◽  
Author(s):  
V.G. Mairanovsky ◽  
S.Kh. Samvelyan
Keyword(s):  
Stopped Flow ◽  
Flow Method

A stopped-flow/continuous-flow method for kinetic determinations

1995 ◽  
Vol 309 (1-3) ◽  
pp. 277-282 ◽  
Author(s):  
Yun-Sheng Hsieh ◽  
S.R. Crouch
Keyword(s):  
Continuous Flow ◽  
Stopped Flow ◽  
Flow Method ◽  
Continuous Flow Method

Acid-catalyzed Hydrolysis of the cis-[Cr(1,10-phenanthroline)2(O2CO)]+ Ion Studied by the u.v.–vis Stopped Flow Method

2006 ◽  
Vol 31 (5) ◽  
pp. 575-579 ◽  
Author(s):  
Dagmara Jacewicz ◽  
Aleksandra Dąbrowska ◽  
Agnieszka Łapińska ◽  
Lech Chmurzyński
Keyword(s):  
Stopped Flow ◽  
Flow Method ◽  
Acid Catalyzed ◽  
Hydrolysis Of

scholarly journals Studies on the reduction of 2,6-dichlorophenolindophenol by 6-substituted 3-hydroxy-4-pyrones, using a stopped-flow method.

1984 ◽  
Vol 48 (11) ◽  
pp. 2615-2619
Author(s):  
Hitoshi OBATA ◽  
Nobuki FUJIWARA ◽  
Jun-ichi TANISHITA ◽  
Tai TOKUYAMA
Keyword(s):  
Stopped Flow ◽  
Flow Method

scholarly journals Kinetic Studies of the Interaction of Toluidine Blue with Poly-(αL-glutamic acid) by Means of Stopped-Flow Method

1978 ◽  
Vol 10 (2) ◽  
pp. 153-159 ◽  
Author(s):  
Hidetoshi Ushio ◽  
Hiroshi Uchimura ◽  
Yoshikuni Tsuji ◽  
Takayuki Sano ◽  
Tatsuya Yasunaga
Keyword(s):  
Glutamic Acid ◽  
Toluidine Blue ◽  
Kinetic Studies ◽  
Stopped Flow ◽  
Flow Method

scholarly journals Study of the Bluing Mechanism of Amylose-Iodine Complexes by CD Stopped-Flow Method.

1991 ◽  
Vol 48 (8) ◽  
pp. 525-528
Author(s):  
Takeshi NISHIMURA ◽  
Hirofumi YAJIMA ◽  
Tadahiro ISHII ◽  
Ryuichi ENDO
Keyword(s):  
Stopped Flow ◽  
Flow Method ◽  
Iodine Complexes
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