Substrate-induced Changes in Domain Interaction of Vacuolar H(+)-Pyrophosphatase

Single molecule atomic force microscopy (smAFM) was employed to unfold transmembrane domain interactions of a unique vacuolar H(+)-pyrophosphatase (EC 3.6.1.1) from Vigna radiata. H(+)-Pyrophosphatase is a membrane-embedded homodimeric protein containing a single type of polypeptide and links PP(i)...

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Détails bibliographiques
Publié dans:J Biol Chem
Auteurs principaux: Hsu, Shen-Hsing, Lo, Yueh-Yu, Liu, Tseng-Huang, Pan, Yih-Jiuan, Huang, Yun-Tzu, Sun, Yuh-Ju, Hung, Cheng-Chieh, Tseng, Fan-Gang, Yang, Chih-Wei, Pan, Rong-Long
Format: Artigo
Langue:Inglês
Publié: American Society for Biochemistry and Molecular Biology 2015
Sujets:
Protein Structure and Folding
Accès en ligne:https://ncbi.nlm.nih.gov/pmc/articles/PMC4294485/
https://ncbi.nlm.nih.gov/pubmed/25451931
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M114.568139
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