Preferential domain orientation of HMGB2 determined by the weak intramolecular interactions mediated by the interdomain linker

Article ID	Journal	Published Year	Pages	File Type
5373989	Chemical Physics	2013	12 Pages	PDF

Abstract

âº Preferential domain arrangement of the domains in HMGB2 in solution was determined. âº The preferential domain orientation was mediated the intramolecular interaction. âº Combined use of RPCSA and SAXS was effective for the structure analysis of a modular Protein.

Keywords

Flexible linker CH-π interaction HSQC NOE SAXS HMGB2 Residual dipolar coupling nuclear overhauser effect transverse relaxation optimized spectroscopy TROSY Domain orientation Diorite Rdc NMR spectroscopy Small-angle X-ray scattering High-mobility group protein heteronuclear single quantum coherence

Related Topics

Physical Sciences and Engineering Chemistry Physical and Theoretical Chemistry

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Preferential domain orientation of HMGB2 determined by the weak intramolecular interactions mediated by the interdomain linker

Authors

Jun-ichi Uewaki, Hironari Kamikubo, Jun-ichi Kurita, Noriteru Hiroguchi, Hiroshi Moriuchi, Michiteru Yoshida, Mikio Kataoka, Naoko Utsunomiya-Tate, Shin-ichi Tate,