ePrints@IIScePrints@IISc Home | About | Browse | Latest Additions | Advanced Search | Contact | Help

Synthetic peptide models for the redox-active disulfide loop of glutaredoxin. Conformational studies

Kishore, R and Raghothama, S and Balaram, P (1988) Synthetic peptide models for the redox-active disulfide loop of glutaredoxin. Conformational studies. In: Biochemistry, 27 (7). pp. 2462-2471.

[img] PDF
Synthetic_Peptide.pdf - Published Version
Restricted to Registered users only

Download (2MB) | Request a copy
Official URL: http://pubs.acs.org/doi/abs/10.1021/bi00407a032


Two cyclic peptide disulfides Boc-Cys-Pro-X-Cys-NHMe (X = L-Tyr or L-Phe) have been synthesized as models for the 14-membered redox-active disulfide loop of glutaredoxin. 'H NMR studies at 270 MHz in chloroform solutions establish a type I 0-turn conformation for the Pro-X segment in both peptides, stabilized by a 4-1 hydrogen bond between the Cys(1) CO and Cys(4) NH groups. Nuclear Overhauser effects establish that the aromatic ring in the X = Phe peptide is oriented over the central peptide unit. In dimethyl sulfoxide solutions two conformational species are observed in slow exchange on the NMR time scale, for both peptides. These are assigned to type I and type I1 p-turn structures with -Pro-Tyr(Phe)-as the corner residues. The structural assignments are based on correlation of NMR parameters with model 14-membered cyclic cystine peptides with Pro-X spacers. Circular dichroism studies based on the -S-Sn- u* transition suggest a structural change in the disulfide bridge with changing solvent polarity, establishing conformational coupling between the peptide backbone and the disulfide linkage in these systems.

Item Type: Journal Article
Publication: Biochemistry
Publisher: American Chemical Society
Additional Information: Copyright of this article belongs to American Chemical Society.
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Division of Chemical Sciences > Sophisticated Instruments Facility (Continued as NMR Research Centre)
Date Deposited: 11 Oct 2010 08:48
Last Modified: 11 Oct 2010 08:48
URI: http://eprints.iisc.ac.in/id/eprint/33008

Actions (login required)

View Item View Item