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

Journal Article · · Biochemistry; (United States)
DOI:https://doi.org/10.1021/bi00407a032· OSTI ID:5173204
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Two cyclic peptide disulfides have been synthesized as models for the 14-membered redox-active disulfide loop glutaredoxin. /sup 1/H NMR studies at 270 MHz in chloroform solutions establish a type I ..beta..-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 II ..beta..-turn structures with -Pro-Tyr(Phe)-as the corner resides. 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-S-n-sigma* 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.
Research Organization:
Indian Institute of Science, Bangalore
OSTI ID:
5173204
Journal Information:
Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 27:7; ISSN BICHA
Country of Publication:
United States
Language:
English

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Related Subjects

550601* -- Medicine-- Unsealed Radionuclides in Diagnostics
62 RADIOLOGY AND NUCLEAR MEDICINE
BARYONS
CHEMICAL REACTIONS
CHROMATOGRAPHY
CONFORMATIONAL CHANGES
DICHROISM
ELEMENTARY PARTICLES
FERMIONS
HADRONS
MAGNETIC RESONANCE
MOLECULAR STRUCTURE
NUCLEAR MAGNETIC RESONANCE
NUCLEONS
ORGANIC COMPOUNDS
PROTEINS
PROTONS
REDOX REACTIONS
RESONANCE
SEPARATION PROCESSES
THIN-LAYER CHROMATOGRAPHY