Folding-unfolding transitions of Rv3221c on the pressure-temperature plane

Judit Somkuti, Sriyans Jain, Srinivasan Ramachandran, L. Smeller

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Rv3221c is a biotin-binding protein found in Mycobacterium tuberculosis. It has been reported that an elevated temperature is needed for it to adopt a folded conformation. We determined the complete pressure-temperature phase diagram, and determined the thermodynamical parameters of the denaturation. The phase diagram follows well the Hawley theory. The secondary structure of the protein was found to contain predominantly beta sheet. The pressure unfolding was partially reversible, resulting in pressure-sensitive aggregates, besides the correctly refolded and biotin-bound fraction of proteins.

Original languageEnglish
Pages (from-to)250-257
Number of pages8
JournalHigh Pressure Research
Volume33
Issue number2
DOIs
Publication statusPublished - Jun 1 2013

Fingerprint

folding
biotin
proteins
phase diagrams
tuberculosis
biopolymer denaturation
temperature

Keywords

  • intrinsically disordered protein
  • Mycobacterium tuberculosis
  • phase diagram
  • pressure
  • Rv3221c

ASJC Scopus subject areas

  • Condensed Matter Physics

Cite this

Folding-unfolding transitions of Rv3221c on the pressure-temperature plane. / Somkuti, Judit; Jain, Sriyans; Ramachandran, Srinivasan; Smeller, L.

In: High Pressure Research, Vol. 33, No. 2, 01.06.2013, p. 250-257.

Research output: Contribution to journalArticle

Somkuti, Judit ; Jain, Sriyans ; Ramachandran, Srinivasan ; Smeller, L. / Folding-unfolding transitions of Rv3221c on the pressure-temperature plane. In: High Pressure Research. 2013 ; Vol. 33, No. 2. pp. 250-257.
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