NDLI: Salt-induced folding of alkaline denatured creatine kinase under high pH conditions

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Salt-induced folding of alkaline denatured creatine kinase under high pH conditions

Content Provider	Scilit
Author	Yang, Hai-Peng Li, Sen Zhong, Hai-Ning Zhou, Hai-Meng
Copyright Year	1997
Description	The conformational changes of creatine kinase during alkaline unfolding and salt‐induced folding at high pH have been followed by fluorescence emission and circular dichroism spectra. The results obtained show that at low ionic strength, with increasing pH value, creatine kinase denatured gradually to reach the ultimate unfolded conformation in the vicinity of pH 12.7. With the increase of pH from 9.0 to 12.7, the fluorescence emission maximum red shifted from 337 to 355 nm, indicating complete exposure of the buried tryptophan residues to the solvent. The far‐UV CD spectra show that even at pH 12.7, the apparently fully denatured enzyme retains a great part of ordered secondary structure. At pH 12.7 by adding the salt, the relatively unfolded state of denatured enzyme changes into a compact conformational state by hydrophobic collapsing. Folded state induced by salt bound ANS strongly, indicating the existence of increased hydrophobic surface. The above results suggest that the salt‐induced folded state at high pH may be the folded intermediate which exists in the general protein folding, and the larger residual ordered secondary structure might become folded being point on the salt‐induced folding.
Related Links	https://iubmb.onlinelibrary.wiley.com/doi/pdf/10.1080/15216549700201261
Ending Page	267
Page Count	11
Starting Page	257
e-ISSN	15216551
DOI	10.1080/15216549700201261
Journal	IUBMB life
Issue Number	2
Volume Number	41
Language	English
Publisher	Informa UK Limited
Publisher Date	1997-02-01
Access Restriction	Open
Subject Keyword	Biophysics Creatine Kinase Alkaline Denaturation Refolding Molten Globule State
Content Type	Text
Resource Type	Article

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