Proteomics

Chaperone-like activity of MTB Hsp16.3 does not require its intact structures

Published in Proteomics Weekly, November 14th, 2005

Chaperone-like activity of Mycobacterium tuberculosis Hsp16.3 does not require its intact structures.

According to recent research published in the journal Biochemistry - Moscow, "Small heat shock proteins (sHsps) were found to exhibit efficient chaperone-like activities under stress conditions although their native structures are severely disturbed.

"Here, using an alternative approach (site-directed mutagenesis), we obtained two structurally and functionally distinct Mycobacterium tuberculosis Hsp16.3 single-site mutant proteins."

"The G59W mutant protein (with Gly59 substituted by Trp) is capable of...

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Source: Proteomics Weekly (2005-11-14)

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