Functional expression, monodispersity and conformational changes in the SBMV virus viral VPg on binding TFE.

Abstract:

:Southern bean mosaic virus (SBMV) RNA purified from infected plants was used for cloning the viral genome-linked protein (VPg) and was subsequently expressed in Escherichia coli. Circular dichroism (CD), dynamic light scattering (DLS) and saturation transfer difference (STD) by nuclear magnetic resonance (NMR) measurements were employed to determine the degree of monodispersity and to investigate the conformational changes in the absence and presence of trifluoroethanol (TFE) which indicated increased helical content with increasing concentration of TFE. 8-Anilino-1-naphthalenesulfonic acid (ANS) was used as a probe to compare the unfolding regions of the protein before and after addition of TFE. The results indicated that although the TFE concentration influences VPg folding, it does not play a role in nucleotide binding and that the local solvent hydrophobicity causes significant conformational changes.

journal_name

Int J Biol Macromol

authors

Mariutti RB,Caruso IP,Ullah A,De Morais FR,Rehders D,Arni RK

doi

10.1016/j.ijbiomac.2015.11.026

subject

Has Abstract

pub_date

2016-02-01 00:00:00

pages

178-84

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(15)30118-5

journal_volume

83

pub_type

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