Events in the kinetic folding pathway of a small, all beta-sheet protein.

The Journal of Biological Chemistry
T SivaramanC Yu

Abstract

The folding of cardiotoxin analogue III (CTX III), a small (60 amino acids), all beta-sheet protein from the venom of the Taiwan Cobra (Naja naja atra) is here investigated. The folding kinetics is monitored by using a variety of techniques such as NMR, fluorescence, and circular dichroism spectroscopy. The folding of the protein is complete within a time scale of 200 ms. The earliest detectable event in the folding pathway of CTX III is the formation of a hydrophobic cluster, which possess strong affinity to bind to nonpolar dye such as 1-anilino-8-napthalene-sulfonic acid. Quenched-flow deuterium-hydrogen exchange experiments indicate that the segment spanning residues 51-55 along with Lys23, Ile39, Val49, Tyr51 and Val52 could constitute the "hydrophobic cluster." Folding kinetics of CTX III based on the amide-protection data reveals that the triple-stranded, antiparallel beta-sheet segment, which is located in the central core of the molecule, appears to fold faster than the double-stranded beta-sheet segment.

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Citations

Sep 20, 2006·Accounts of Chemical Research·David EisenbergChristian Riekel
Aug 9, 2012·Langmuir : the ACS Journal of Surfaces and Colloids·Dianlu JiangFeimeng Zhou
Jun 10, 2005·Nature·Rebecca NelsonDavid Eisenberg
Aug 19, 1999·Protein Science : a Publication of the Protein Society·R Li, C Woodward
Nov 12, 2014·Journal of Biomolecular Structure & Dynamics·Biswajit GoraiThirunavukkarasu Sivaraman
Jun 12, 2013·Acta Biochimica Et Biophysica Sinica·Yannan BinJuan Xiang
Oct 23, 2009·Proteins·Mirco Junker, Patricia L Clark
Oct 20, 2000·The Journal of Biological Chemistry·D SamuelC Yu
Dec 22, 2004·Accounts of Chemical Research·Thallapuranam Krishnaswamy S Kumar, Chin Yu

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