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Comparative folding analyses of unknotted versus trefoil-knotted ornithine transcarbamylases suggest stabilizing effects of protein knots.
Sriramoju, Manoj Kumar; Yang, Tzu-Jing; Hsu, Shang-Te Danny.
Affiliation
  • Sriramoju MK; Institute of Biological Chemistry, Academia Sinica, Taipei, 11529, Taiwan.
  • Yang TJ; Institute of Biological Chemistry, Academia Sinica, Taipei, 11529, Taiwan; Institute of Biochemical Sciences, National Taiwan University, Taipei, 10617, Taiwan.
  • Hsu SD; Institute of Biological Chemistry, Academia Sinica, Taipei, 11529, Taiwan; Institute of Biochemical Sciences, National Taiwan University, Taipei, 10617, Taiwan. Electronic address: sthsu@gate.sinica.edu.tw.
Biochem Biophys Res Commun ; 503(2): 822-829, 2018 09 05.
Article in En | MEDLINE | ID: mdl-29920242
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Ornithine Carbamoyltransferase / Bacterial Proteins / Protein Folding / Protein Structure, Quaternary Language: En Journal: Biochem Biophys Res Commun Year: 2018 Document type: Article Affiliation country: Taiwan Country of publication: United States
Fulltext
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Ornithine Carbamoyltransferase / Bacterial Proteins / Protein Folding / Protein Structure, Quaternary Language: En Journal: Biochem Biophys Res Commun Year: 2018 Document type: Article Affiliation country: Taiwan Country of publication: United States