Abstract:
: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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Constantine KL,Friedrichs MS,Bell AJ,Lavoie TB,Mueller L,Metzler WJdoi
10.1016/0014-5793(93)80855-osubject
Has Abstractpub_date
1993-12-28 00:00:00pages
457-61issue
3eissn
0014-5793issn
1873-3468pii
0014-5793(93)80855-Ojournal_volume
336pub_type
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