Complement assembly of two fragments of the streptococcal protein G B1 domain in aqueous solution

FEBS Letters

Honda, Shinya²  Kobayashi, Naohiro¹  Yoshii, Hirofumi¹  Uedaira, Hatsuho²  Munekata, Eisuke¹ 

[1] Institute of Applied Biochemistry, University of Tsukuba, Tsukuba 305, Japan;National Institute of Bioscience and Human-Technology, Tsukuba 305, Japan

关键词: Protein G;    Protein folding;    Complementation;    Nuclear magnetic resonance;    Circular dichroism;    CD;    circular dichroism;    d aN(ij);    intramolecular distance between the protons CαH and NH on the residues i and j;    DQF-COSY;    two-dimensional double quantum-filtered coherence transfer spectroscopy;    HOHAHA;    two-dimensional homo-nuclear Hartmann-Hahn spectroscopy;    K d;    dissociation constant;    NOESY;    two-dimensional nuclear Overhauser and exchange spectroscopy;    PGB1;    protein G B1 domain;    ROESY;    two-dimensional rotating frame nuclear Overhauser and exchange spectroscopy;    [x + y];    equimolar mixture of fragments x and y;    NMR;    nuclear magnetic resonance;   

DOI  :  10.1016/0014-5793(95)00503-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We examined the complementation of various pairs of fragments derived from the streptococcal protein G B1 domain by NMR and CD. Most were not associated; however, one pair of fragments (1–40) and (41–56) interacted sufficiently enoughto regenerate a stable 1:1 complex, K _d = 9 × 10⁻⁶M. A 2D-NMR analysis showed that the structure of the complex resembled that of native domain. Here we discuss the complementation from the viewpoint of the folding pathway of the protein.

【 授权许可】

Unknown