STRUCTURES OF WILD-TYPE AND MUTANT SIGNAL SEQUENCES OF ESCHERICHIA-COLI RIBOSE BINDING-PROTEIN

The structure of a chemically synthesized 25-residue-long functional signal peptide of Escherichia coli ribose binding protein was compared with that of a nonfunctional mutant-signal peptide using circular dichroism and two-dimensional H-1 NMR in solvents mimicking the amphiphilic environments. The functional peptide forms an 18-residue-long alpha-helix starting from the NH2-terminal region and reaching to the hydrophobic stretch in a solvent consisting of 10% dimethylsulfoxide, 40% water, and 50% trifluoroethanol (v/v). The nonfunctional mutant peptide, which contains a Pro at position 9 instead of a Leu in the wild-type peptide, does not have any secondary structure in that solvent but forms a 12-residue-long alpha-helix within the hydrophobic stretch in water/trifluoroethanol (50:50, v/v) solvent. It seems that the Pro-9 residue in the nonfunctional peptide disturbs the helix propagation from the hydrophobic stretch to the NH2-terminal region. Because both of these peptides have stable helices within the hydrophobic stretch, it may be concluded that the additional 2 turns of the alpha-helix in the NH2-terminal region of the wild-type signal peptide is important for its function.
Publisher
BIOPHYSICAL SOCIETY
Issue Date
1994-05
Language
ENG
Keywords

NUCLEAR-MAGNETIC-RESONANCE; PROTON PROTON DISTANCES; CIRCULAR-DICHROISM; H-1-NMR SPECTRA; SPECTROSCOPY; CONFORMATION; PEPTIDES; STABILITY; EXPORT; MODEL

Citation

BIOPHYSICAL JOURNAL, v.66, no.5, pp.1604 - 1611

ISSN
0006-3495
URI
http://hdl.handle.net/10203/65371
Appears in Collection
BiS-Journal Papers(저널논문)CH-Journal Papers(저널논문)BS-Journal Papers(저널논문)
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