BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

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Entry ID Data summary Entry Title Citation Title Authors
17066 Chemical Shifts: 1 set
SOLUTION NMR STRUCTURE OF THE N-TERMINAL PAS DOMAIN OF HERG POTASSIUM CHANNEL The N-terminal tail of hERG contains an amphipathic -helix that regulates channel deactivation. Download bibtex for citation iamge Chai Ann Ng, Daniela Stock, Glenn F King, Jamie I Vandenberg, Mark J Hunter, Matthew D Perry, Mehdi Mobli, Philip W Kuchel, Ying Ke
5922 Chemical Shifts: 1 set
Solution Structure of the HERG K+ channel S5-P extracellular linker Structure of the HERG K+ channel S5P extracellular linker: Role of an amphipathic alpha-helix in c-type inactivation Download bibtex for citation iamge A Bauskin, A M Torres, C E Clarke, D J Smith, J A Bursill, J I Vandenberg, M Sunde, P F Alewood, P S Bansal, P W Kuchel, S N Breit, T J Campbell