Effect of prolyl isomerase on the folding reactions of staphylococcal nuclease

scientific article published on 01 December 1997

Effect of prolyl isomerase on the folding reactions of staphylococcal nuclease is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1021/BI971357R
P698PubMed publication ID9398241

P2093author name stringFink AL
Nall BT
Veeraraghavan S
P433issue49
P407language of work or nameEnglishQ1860
P304page(s)15134-15139
P577publication date1997-12-01
P1433published inBiochemistryQ764876
P1476titleEffect of prolyl isomerase on the folding reactions of staphylococcal nuclease
P478volume36

Reverse relations

cites work (P2860)
Q37512448An Intracellular Peptidyl-Prolyl cis/trans Isomerase Is Required for Folding and Activity of the Staphylococcus aureus Secreted Virulence Factor Nuclease
Q30430775Antibody catalysis of peptidyl-prolyl cis-trans isomerization in the folding of RNase T1.
Q28346214Decomposition of protein tryptophan fluorescence spectra into log-normal components. III. Correlation between fluorescence and microenvironment parameters of individual tryptophan residues
Q43032857Functional analysis of the Glucan Degradation Locus (GDL) in Caldicellulosiruptor bescii reveals essential roles of component glycoside hydrolases in plant biomass deconstruction
Q78168242Proline isomerization is unlikely to be the cause of slow annealing and reactivation during the folding of alkaline phosphatase
Q34545614Prolyl isomerases
Q42846959Thermodynamic analysis of halide binding to haloalkane dehalogenase suggests the occurrence of large conformational changes

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