| Title: | Long-distance rotational echo double resonance measurements for the determination of secondary structure and conformational heterogeneity in peptides |
| Author(s): | Arshava B; Breslav M; Antohi O; Stark RE; Garbow JR; Becker JM; Naider F; |
| Address: | "Department of Chemistry, College of Staten Island and the Graduate School of the City University of New York, 10314, USA" |
| Journal Title: | Solid State Nucl Magn Reson |
| DOI: | 10.1016/s0926-2040(99)00018-1 |
| ISSN/ISBN: | 0926-2040 (Print) 0926-2040 (Linking) |
| Abstract: | "The utility of rotational echo double resonance (REDOR) NMR spectroscopy for determining the conformations of linear peptides has been examined critically using a series of crystalline and amorphous samples. The focus of the present work was the evaluation of long-distance (> 5 A) interactions using 13C-15N dephasing. Detailed studies of specifically labeled melanostatin and synthetic analogs of the alpha-factor yeast mating hormone show that nitrogen-dephased, carbon-observe REDOR measurements are reliable for distances up to 6.0 A, and that dipolar interactions can be detected for distances up to 7 A. By contrast, nitrogen-observe REDOR gives reliable results only for distances shorter than 5.0 A. To measure distances accurately, REDOR data must be corrected for the effects of natural-abundance spins. These corrections are particularly important for measuring long distances, which are of the greatest value for determining peptide secondary structure. We have developed a spherical shell model for calculating the effect of these background spins. The REDOR studies also indicate that in a lyophilized powder, the tridecapeptide alpha-factor mating pheromone from Saccharomyces cerevisiae (WHWLQLKPGQPMY) probably exists as a distribution of different turn structures around the KPGQ region. This finding revises previous solid-state NMR studies on this peptide, which concluded alpha-factor assumes a distorted type-I beta-turn in the Pro-Gly central region of the molecule [J.R. Garbow, M. Breslav, O. Antohi, F. Naider, Biochemistry, 33 (1994) 10094]" |
| Keywords: | "Algorithms Amino Acid Sequence Chromatography, High Pressure Liquid Freeze Drying Magnetic Resonance Spectroscopy Molecular Sequence Data Peptides/chemical synthesis/*chemistry Protein Conformation Protein Structure, Secondary;" |
| Notes: | "MedlineArshava, B Breslav, M Antohi, O Stark, R E Garbow, J R Becker, J M Naider, F eng GM22086/GM/NIGMS NIH HHS/ GM22087/GM/NIGMS NIH HHS/ Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Netherlands 1999/08/07 Solid State Nucl Magn Reson. 1999 Jul; 14(2):117-36. doi: 10.1016/s0926-2040(99)00018-1" |
