Open AccessComplete 1H, 13C, 15N resonance assignments and secondary structure of the Vpr binding region of hHR23A (residues 223–363)
Author(s) -
InJa L. Byeon,
Jinwon Jung,
Chang H Byeon,
Maria DeLucia,
Jin-Woo Ahn,
Angela M. Gronenborn
Publication year - 2019
Publication title -
biomolecular nmr assignments
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.359
H-Index - 16
eISSN - 1874-2718
pISSN - 1874-270X
DOI - 10.1007/s12104-019-09913-x
Subject(s) - heteronuclear single quantum coherence spectroscopy , protein secondary structure , resonance (particle physics) , side chain , chemistry , protein structure , crystallography , nuclear magnetic resonance , two dimensional nuclear magnetic resonance spectroscopy , stereochemistry , physics , biochemistry , atomic physics , organic chemistry , polymer
Comprehensive resonance assignments and delineation of the secondary structure elements of the C-terminal Vpr-binding region of hHR23A, residues 223-363, were achieved by triple-resonance NMR experiments on uniformly 13 C, 15 N-labeled protein. Assignments are 100% and > 95% complete for backbone and side-chain resonances, respectively. This data constitutes important complementary information for our ongoing structure determination of the Vpr-hHR23A(223-363) complex. At high concentrations, severe line-broadening was observed for several residues in the 1 H- 15 N HSQC spectrum, most likely resulting from inter-molecular interactions.