CIRCULAR-DICHROISM OF DENATURED BARSTAR SUGGESTS RESIDUAL STRUCTURE

Authors
NOLTING B GOLBIK R SOLERGONZALEZ AS FERSHT AR
Citation
B. Nolting et al., CIRCULAR-DICHROISM OF DENATURED BARSTAR SUGGESTS RESIDUAL STRUCTURE, Biochemistry, 36(32), 1997, pp. 9899-9905
Citations number
50
Categorie Soggetti
Biology
Journal title
Biochemistry → ACNP
ISSN journal
00062960
Volume
36
Issue
32
Year of publication
1997
Pages
9899 - 9905
Database
ISI
SICI code
0006-2960(1997)36:32<9899:CODBSR>2.0.ZU;2-R
Abstract
The circular dichroism (CD) spectrum of the denatured state of barstar has been analyzed as a function of urea and temperature. The near-and far-UV CD spectra change very rapidly in magnitude and shape with inc reasing temperature, unlike those of native protein, suggesting the pr esence of residual structure that changes with denaturing conditions. The effect of mutations indicates that there is residual. structure in helix(1) of the protein, consistent with NMR data. The changes in CD with conditions are consistent with the denatured state being a mixtur e of conformations of similar energy.