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
50998 Chemical Shifts: 2 sets
Backbone assignment of human prolactin at pH 7.0 and 5.5 Architecture of the two metal binding sites in prolactin Download bibtex for citation iamge Camille Keeler, Dmitry M Korzhnev, Janus Vang, Jeffrey C Hoch, Michael E Hodsdon, Oksana Gorbatyuk, Yulia Pustovalova
25029 Chemical Shifts: 1 set
Specific and Non-Specific Interactions in Ultra-Weak Protein-Protein Associations Revealed by Solvent Paramagnetic Relaxation Enhancements Specific and nonspecific interactions in ultraweak protein-protein associations revealed by solvent paramagnetic relaxation enhancements. Download bibtex for citation iamge Camille Keeler, Helle Johansson, Henrik Gesmar, Jens J Led, Joachim M Vinther, Malene Ringkjobing R Jensen, Michael E Hodsdon, Sebastian Meier
19633 Chemical Shifts: 1 set
Solution structure of a EF-hand domain from sea urchin polycystin-2 The number and location of EF hand motifs dictates the calcium dependence of polycystin-2 function. Download bibtex for citation iamge Andjelka Celic, Barbara E Ehrlich, Camille Keeler, Edward T Petri, Ivana Y Kuo, Michael E Hodsdon, Rachel Corbin
15773 Chemical Shifts: 4 sets
Analysis of Site-specific Histidine Protonation in Human Prolactin Analysis of Site-specific Histidine Protonation in Human Prolactin Download bibtex for citation iamge Camille Keeler, M Cristina Tettamanzi, Michael E Hodsdon, Syrus Meshack
5599 Chemical Shifts: 1 set
The Tertiary Structure and Backbone Dynamics of Human Prolactin: Evidence for Reversible Oligomerization in Solution The Tertiary Structure and Backbone Dynamics of Human Prolactin Download bibtex for citation iamge Camille Keeler, Michael E Hodsdon, Priscilla S Dannies