The denatured states of ribonuclease-A: mechanism of denaturation by lithium chloride.
Indian J Biochem Biophys
; 1989 Oct; 26(5): 301-4
Article
Dans En
| IMSEAR
| ID: sea-28036
ABSTRACT
Denaturation of ribonuclease-A by lithium chloride has been studied using difference spectral, circular dichroic and viscometric measurements. The difference spectral results were interpreted in the light of our observations that the solvent effect of the denaturant on the tyrosyl residue is non-linear. It has been observed that (1) the lithium chloride-denatured protein contains 3% alpha-helix and 18% beta-structure, and (2) only two of the three buried tyrosyl residues are normalized in the denatured protein.
Texte intégral:
1
Indice:
IMSEAR
Sujet Principal:
Dénaturation des protéines
/
Pancreatic ribonuclease
/
Analyse spectrale
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Viscosité
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Chlorures
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Dichroïsme circulaire
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Chlorure de lithium
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Lithium
langue:
En
Texte intégral:
Indian J Biochem Biophys
Année:
1989
Type:
Article