Improvement of the 2.5 Å resolution model of cytochrome b562 by redetermining the primary structure and using molecular graphics
- 1 June 1981
- journal article
- research article
- Published by Elsevier BV in Journal of Molecular Biology
- Vol. 148 (4), 427-448
- https://doi.org/10.1016/0022-2836(81)90185-6
Abstract
No abstract availableThis publication has 28 references indexed in Scilit:
- Structural comparisons of heme binding proteinsBiochemistry, 1979
- Anomalies in amino acid sequences of small cytochromes c and cytochromes c′ from two species of purple photosynthetic bacteriaNature, 1979
- Protein disk of tobacco mosaic virus at 2.8 Å resolution showing the interactions within and between subunitsNature, 1978
- Circular dichroism and resonance Raman studies of cytochrome b562 from Escherichia coliBiochemistry, 1978
- Electron density map of apoferritin at 2.8-Å resolutionNature, 1978
- Hämoglobin, XXIII. Notiz zur Sequenz der δ-Ketten der menschlichen Hämoglobine (Hb A2= α2/δ2)Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1978
- The Sequence Determination of a Protein in a Micro Scale: The Sequence Analysis of Ribosomal Protein L34 ofEscherichia coliHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1976
- Location of the iron atom and the non-crystallographic symmetry elements in cytochrome b562Journal of Molecular Biology, 1974
- The Diagram, a Method for Comparing SequencesEuropean Journal of Biochemistry, 1970
- DISC ELECTROPHORESIS – II METHOD AND APPLICATION TO HUMAN SERUM PROTEINS*Annals of the New York Academy of Sciences, 1964