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Biological Magnetic Resonance Data BankA Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules |
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Entry ID | Data summary | Entry Title | Citation Title(s) | Authors |
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19702 | Chemical Shifts: 1 set |
Structure of the dimerization domain of the human polyoma, JC virus agnoprotein is an amphipathic alpha-helix. |
1: Human polyomavirus JC small regulatory agnoprotein forms highly stable dimers and oligomers: implications for their roles in agnoprotein function. 2: Nuclear magnetic resonance structure revealed that human polyoma JC virus agnoprotein contains an alpha-helix encompassing the Leu/Ile/Phe-rich domain. 3: Nuclear magnetic resonance structure revealed that human polyoma, JC virus agnoprotein contains an alpha-helix encompassing the Leu/Ile/Phe-rich domain |
A Sami Saribas, E R Viola, Magid Abou-Gharbia, Mahmut Safak, Martyn K White, Martyn White, M K White, M Safak, Pascale Coric, Sami A Saribas, Serge Bouaziz, T B Arachea, Wayne Childers |