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Size of Unfolded and Dissociated Subunits versus that of Native Multimeric Proteins

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Title Size of Unfolded and Dissociated Subunits versus
that of Native Multimeric Proteins
 
Creator Dutta, Samrajnee
Bhattacharyya, Debasish
 
Subject Cancer Biology and Inflammatory Disorder Division
 
Description Two factors, unfolding and dissociation, act in opposition in determining the size of the
unfolded state of multimeric proteins. An analysis has been presented to correlate relative expansion
of the unfolded monomers in absence of disulfide bridges over the native state of different homomultimeric
proteins of varying molecular weights. The Stoke’s radii of about 70 proteins of Mw
between 6 kDa to 4000 kDa and ranging from monomers to dodecamers were calculated both under
native and denatured condition induced by 8 M urea or 6 M guanidinium,HCl according to relations
derived by Uversky [Biochemistry 32 (1993), 13288–13298]. Stoke’s radii of monomeric proteins
were found to increase by 1.6–2.2 times after denaturation as compared with the native state while
that of the subunits of dimeric and tetrameric proteins were increased by factors 1.1–2.2 under the
same conditions. For hexameric proteins this factor lies between 0.96–1.2. In each set the relative
increment of the Stoke’s radii followed a logarithmic relation with molecular weight and reached
a minimum limiting value when Stoke’s radii of native protein became almost equal to that of the
unfolded monomer.
 
Date 2001
 
Type Article
PeerReviewed
 
Format application/pdf
 
Identifier http://www.eprints.iicb.res.in/895/1/JOURNAL_OF_BIOLOGICAL_PHYSICS%2C__27(_1)%2C_59%2D71%2C2001_[69].pdf
Dutta, Samrajnee and Bhattacharyya, Debasish (2001) Size of Unfolded and Dissociated Subunits versus that of Native Multimeric Proteins. Journal of Biological Physics, 27 (1). pp. 59-71.
 
Relation http://dx.doi.org/10.1023/A:1011826525684
http://www.eprints.iicb.res.in/895/