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Journal of molecular biology1968; 35(3); 477-481; doi: 10.1016/s0022-2836(68)80007-5

Comparison of protein structure in the crystal and in solution. V. Solubility of horse methemoglobin and azide binding.

Abstract: No abstract available
Publication Date: 1968-08-14 PubMed ID: 5673693DOI: 10.1016/s0022-2836(68)80007-5Google Scholar: Lookup
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Cite This Article

APA
Rupley JA, Gates V. (1968). Comparison of protein structure in the crystal and in solution. V. Solubility of horse methemoglobin and azide binding. J Mol Biol, 35(3), 477-481. https://doi.org/10.1016/s0022-2836(68)80007-5

Publication

ISSN: 0022-2836
NlmUniqueID: 2985088R
Country: Netherlands
Language: English
Volume: 35
Issue: 3
Pages: 477-481

Researcher Affiliations

Rupley, J A
    Gates, V

      MeSH Terms

      • Animals
      • Azides
      • Crystallization
      • Crystallography
      • Horses
      • In Vitro Techniques
      • Methemoglobin
      • Protein Binding
      • Solubility
      • Spectrophotometry

      Citations

      This article has been cited 1 times.
      1. Calvey GD, Katz AM, Zielinski KA, Dzikovski B, Pollack L. Characterizing Enzyme Reactions in Microcrystals for Effective Mix-and-Inject Experiments using X-ray Free-Electron Lasers.. Anal Chem 2020 Oct 20;92(20):13864-13870.
        doi: 10.1021/acs.analchem.0c02569pubmed: 32955854google scholar: lookup