Solution 1H nuclear magnetic resonance determination of hydrogen bonding of the E10 (66) Arg side-chain to the bound ligand in Aplysia cyano-met myoglobin
- 20 April 1992
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 224 (4) , 891-897
- https://doi.org/10.1016/0022-2836(92)90456-t
Abstract
No abstract availableKeywords
This publication has 22 references indexed in Scilit:
- Proton nuclear magnetic resonance study of the solution distal histidine orientation in monomeric Chironomus thummi thummi cyanomet hemoglobins: Dynamic stability of the heme pocket as monitored by Labile proton exchangeJournal of Molecular Biology, 1991
- Control and recognition of anionic ligands in myoglobinFEBS Letters, 1991
- Binding mode of azide to ferricAplysia limacina myoglobin. Crystallographic analysis at 1.9 Å resolutionJournal of Molecular Recognition, 1991
- X-ray crystal structure of the fluoride derivative of Aplysia limacina ferric myoglobin at 2·0 Å resolutionJournal of Molecular Biology, 1990
- Proton nuclear magnetic resonance study of the molecular and electronic structure of the heme cavity in Aplysia cyanometmyoglobinBiochemistry, 1989
- Aplysia limacina myoglobinJournal of Molecular Biology, 1989
- The role of the distal histidine in myoglobin and haemoglobinNature, 1988
- Refinement of a molecular model for lamprey hemoglobin from Petromyzon marinusJournal of Molecular Biology, 1985
- Structure of human oxyhaemoglobin at 2·1resolutionJournal of Molecular Biology, 1983
- Real space refinement of neutron diffraction data from sperm whale carbonmonoxymyoglobinJournal of Molecular Biology, 1981