13C-{1H} NMR/NOE and Multiplet Relaxation Data in Modeling Protein Dynamics of a Collagen 13C-Enriched Glycine GXX Repeat Motif Hexadecapeptide

Vladimir A. Daragan, Kevin H. Mayo

Research output: Contribution to journalArticlepeer-review

15 Scopus citations

Abstract

13C-NMR (75 MHz) multiple! spin-lattice (T1) relaxation and 13-{1H} nuclear Overhauser measurements have been performed on a 13C-glycine-XX repeating hexadecapeptide, i.e., GVKGDKGNPGWPGAPY, from the triple helix domain of collagen type IV. The data have been analyzed using a formalism that considers both autocorrelation and cross-correlation dipolar spectral densities. Several motional models were tested for consistency with the data. The terminal glycine, G1, and nonterminal glycines, G4, G7, G10, and G13, were found to have distinctly different motional properties that could not be explained simultaneously by any one model. Results indicate that most glycines rotate more isotropically than the N-terminal glycine. Analysis of the experimental data using several rotational models indicates that internal motions in the peptide are important to terminal, as well as nonterminal, 13C-glycine relaxation. The character of the rotational motion of nonterminal glycines varies considerably with temperature. Although simple rotational diffusion models can describe terminal glycine motion, consideration of multiple internal rotations are necessary to fully describe nonterminal glycine rotations.

Original languageEnglish (US)
Pages (from-to)4326-4331
Number of pages6
JournalJournal of the American Chemical Society
Volume114
Issue number11
DOIs
StatePublished - May 1 1992
Externally publishedYes

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