Conformational and dynamic properties of a 14 residue antifreeze glycopeptide from antarctic cod

• Published in: Protein Science
• Main Authors: Lane, Andrew N., Hays, Lisa M., Crowe, Lois M., Crowe, John H., Feeney, Robert E.
• Format: Article in Journal/Newspaper
• Language: English
• Published: Wiley 1998
• Subjects: Antarctic; Antarc*
• Online Access: http://dx.doi.org/10.1002/pro.5560070709; https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fpro.5560070709; https://onlinelibrary.wiley.com/doi/pdf/10.1002/pro.5560070709

Abstract The 1 H and 13 C NMR spectra of a 14‐residue antifreeze glycopeptide from Antarctic cod ( Tetramatornus horchgrevinki ) containing two proline residues have been assigned. 13 C NMR relaxation experiments indicate motional anisotropy of the peptide, with a tumbling time in water at 5 °C of 3‐4 ns. The relaxation data and lack of long‐range NOEs are consistent with a linear peptide undergoing significant segmental motion. However, extreme values of some coupling constants and strong sequential NOEs indicate regions of local order, which are most evident at the two ATPA subsequences. Similar spectroscopic properties were observed in the 16‐residue analogue containing an Arg‐Ala dipeptide added to the C‐terminus. Molecular modeling also showed no evidence of long‐range order, but the two ATPA subsequences were relatively well determined by the experimental data. These motifs were quite distinct from helical structures or β turns commonly found in proteins, but rather resemble sections of an extended polyproline helix. Thus, the NMR data provide a description of the local order, which is of relevance to the mechanism of action of the antifreeze activity of the antifreeze glycopeptides as well as their ability to protect cells during hypothermic storage.