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Literature summary for 4.6.1.24 extracted from

  • Alston, R.W.; Lasagna, M.; Grimsley, G.R.; Scholtz, J.M.; Reinhart, G.D.; Pace, C.N.
    Tryptophan fluorescence reveals the presence of long-range interactions in the denatured state of ribonuclease Sa (2008), Biophys. J., 94, 2288-2296.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
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Kitasatospora aureofaciens

Protein Variants

Protein Variants Comment Organism
D1W the mutant is studied in concentrated urea and GdnHCl solution with their disulfide bond broken, the results show that long-range effects in a denaturated protein can significantly effect the fluorescence properties Kitasatospora aureofaciens
T76W the mutant is studied in concentrated urea and GdnHCl solution with their disulfide bond broken, the results show that long-range effects in a denaturated protein can significantly effect the fluorescence properties Kitasatospora aureofaciens
Y52W the mutant is studied in concentrated urea and GdnHCl solution with their disulfide bond broken, the results show that long-range effects in a denaturated protein can significantly effect the fluorescence properties Kitasatospora aureofaciens
Y55W the mutant is studied in concentrated urea and GdnHCl solution with their disulfide bond broken, the results show that long-range effects in a denaturated protein can significantly effect the fluorescence properties Kitasatospora aureofaciens
Y81W the mutant is studied in concentrated urea and GdnHCl solution with their disulfide bond broken, the results show that long-range effects in a denaturated protein can significantly effect the fluorescence properties Kitasatospora aureofaciens

Organism

Organism UniProt Comment Textmining
Kitasatospora aureofaciens
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-
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Purification (Commentary)

Purification (Comment) Organism
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Kitasatospora aureofaciens

Synonyms

Synonyms Comment Organism
Ribonuclease SA
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Kitasatospora aureofaciens
RNase Sa
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Kitasatospora aureofaciens