Relaxation study of the backbone dynamics of human profilin by two-dimensional 1H-15N NMR.
Related Articles Relaxation study of the backbone dynamics of human profilin by two-dimensional 1H-15N NMR.
FEBS Lett. 1993 Dec 28;336(3):457-61
Authors: Constantine KL, Friedrichs MS, Bell AJ, Lavoie TB, Mueller L, Metzler WJ
The dynamic properties of 111 backbone HN sites in uncomplexed human profilin, a protein of 139 residues, have been characterized by two-dimensional inverse-detected 1H-15N NMR spectroscopy. Heteronuclear (1H)-15N nuclear Overhauser effects and 15N longitudinal and transverse relaxation rates have been analyzed in terms of model-free spectral density functions and exchange contributions to transverse relaxation rates. Relatively high mobilities on the nanosecond time-scale are observed for Asp26 and Ser27, which form part of a loop connecting beta-strands A and B, and for Thr92 through Ala95, which are in a loop connecting beta-strands E and F. Significant exchange contributions, indicative of motions on the microsecond to millisecond time-scale, have been obtained for 30 residues. These include Leu77, Asp80 and Gly81 of a loop between beta-strands D and E, Ser84 and Met85 of beta-strand E, Gly121 of a loop connecting beta-strand G and the C-terminal helix, and Gln138, which is next to the C-terminal residue Tyr139. Some of the regions showing high flexibility in profilin are known to be involved in poly-L-proline binding.
PMID: 8282110 [PubMed - indexed for MEDLINE]
Source:
PubMed