Characterization of Threonine Side Chain Dynamics in an Antifreeze Protein Using Natural Abundance 13C NMR Spectroscopy

Overview

Journal J Biomol NMR

Publisher Springer

Specialties Molecular Biology
Nuclear Medicine

Date 2004 Mar 12

PMID 15014228

Citations 2

Authors

Margaret E Daley

Brian D Sykes

Affiliations

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Abstract

The dynamics of threonine side chains of the Tenebrio molitor antifreeze protein (TmAFP) were investigated using natural abundance (13)C NMR. In TmAFP, the array of threonine residues on one face of the protein is responsible for conferring its ability to bind crystalline ice and inhibit its growth. Heteronuclear longitudinal and transverse relaxation rates and the [(1)H]-(13)C NOE were determined in this study. The C alpha H relaxation measurements were compared to the previously measured (15)N backbone parameters and these are found to be in agreement. For the analysis of the threonine side chain motions, the model of restricted rotational diffusion about the chi(1) dihedral angle was employed [London and Avitabile (1978) J. Am. Chem. Soc., 100, 7159-7165]. We demonstrate that the motion experienced by the ice binding threonine side chains is highly restricted, with an approximate upper limit of less than +/-25 degrees.

Citing Articles

Long-range protein-water dynamics in hyperactive insect antifreeze proteins.

Meister K, Ebbinghaus S, Xu Y, Duman J, DeVries A, Gruebele M Proc Natl Acad Sci U S A. 2013; 110(5):1617-22.

PMID: 23277543 PMC: 3562781. DOI: 10.1073/pnas.1214911110.

NMR characterizations of the ice binding surface of an antifreeze protein.

Hong J, Hu Y, Li C, Jia Z, Xia B, Jin C PLoS One. 2011; 5(12):e15682.

PMID: 21209943 PMC: 3011014. DOI: 10.1371/journal.pone.0015682.

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