Effects of polyamines and analogs on staphylococcal nuclease

1976 ◽  
Vol 16 (8) ◽  
pp. 627-632 ◽  
Author(s):  
H. Yanagawa ◽  
Y. Ogawa ◽  
F. Egami
Keyword(s):  
Staphylococcal Nuclease

scholarly journals Modification of the Single Tryptophan Residue of Staphylococcal Nuclease by a New Mild Oxidizing Agent

1970 ◽  
Vol 245 (8) ◽  
pp. 1895-1902 ◽  
Author(s):  
Gilbert S. Omenn ◽  
Angelo Fontana ◽  
Christian B. Anfinsen
Keyword(s):  
Staphylococcal Nuclease ◽  
Tryptophan Residue ◽  
Oxidizing Agent

scholarly journals The ompA signal peptide directed secretion of Staphylococcal nuclease A by Escherichia coli.

1985 ◽  
Vol 260 (5) ◽  
pp. 2670-2674 ◽  
Author(s):  
M Takahara ◽  
D W Hibler ◽  
P J Barr ◽  
J A Gerlt ◽  
M Inouye
Keyword(s):  
Escherichia Coli ◽  
Signal Peptide ◽  
Staphylococcal Nuclease

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 Correlation between the Antigenic and Catalytic Properties of Staphylococcal Nuclease

1969 ◽  
Vol 244 (4) ◽  
pp. 943-950 ◽  
Author(s):  
S Fuchs ◽  
P Cuatrecasas ◽  
D A Ontjes ◽  
C B Anfinsen
Keyword(s):  
Catalytic Properties ◽  
Staphylococcal Nuclease

scholarly journals Crystallization and preliminary X-ray analysis of a quadruple mutant of staphylococcal nuclease.

1988 ◽  
Vol 263 (34) ◽  
pp. 18190-18192
Author(s):  
P J Loll ◽  
A K Meeker ◽  
D Shortle ◽  
M Pease ◽  
E E Lattman
Keyword(s):  
Staphylococcal Nuclease ◽  
X Ray ◽  
Quadruple Mutant

scholarly journals The Interaction of Nucleotides with the Active Site of Staphylococcal Nuclease

1967 ◽  
Vol 242 (20) ◽  
pp. 4759-4767 ◽  
Author(s):  
Pedro Cuatrecasas ◽  
Sara Fuchs ◽  
Christian B. Anfinsen
Keyword(s):  
Active Site ◽  
Staphylococcal Nuclease
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