Literature DB >> 19636940

1H, 15N and 13C assignments of domain 5 of Dictyostelium discoideum gelation factor (ABP-120) in its native and 8M urea-denatured states.

Shang-Te Danny Hsu1, Lisa D Cabrita, John Christodoulou, Christopher M Dobson.   

Abstract

The gelation factor from Dictyostelium discoideum (ABP-120) is an actin binding protein consisting of six immunoglobulin (Ig) domains in the C-terminal rod domain. We have recently used the pair of domains 5 and 6 of ABP-120 as a model system for studying multi-domain nascent chain folding on the ribosome. Here we present the NMR assignments of domain 5 in its native and 8M urea-denatured states.

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Year:  2008        PMID: 19636940     DOI: 10.1007/s12104-008-9134-4

Source DB:  PubMed          Journal:  Biomol NMR Assign        ISSN: 1874-270X            Impact factor:   0.746


  2 in total

1.  A molten globule-to-ordered structure transition of Drosophila melanogaster crammer is required for its ability to inhibit cathepsin.

Authors:  Tien-Sheng Tseng; Chao-Sheng Cheng; Dian-Jiun Chen; Min-Fang Shih; Yu-Nan Liu; Shang-Te Danny Hsu; Ping-Chiang Lyu
Journal:  Biochem J       Date:  2012-03-15       Impact factor: 3.857

2.  Entropic stabilization of a deubiquitinase provides conformational plasticity and slow unfolding kinetics beneficial for functioning on the proteasome.

Authors:  Yun-Tzai Cloud Lee; Chia-Yun Chang; Szu-Yu Chen; Yun-Ru Pan; Meng-Ru Ho; Shang-Te Danny Hsu
Journal:  Sci Rep       Date:  2017-03-24       Impact factor: 4.379

  2 in total

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