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Structural Differences Between Rate States of Carboxyhemoglobin Compounds

  • Chapter
Protein Structure

Part of the book series: Proceedings in Life Sciences ((LIFE SCIENCES))

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Abstract

The two state model of hemoglobin has been popular for many years but the description of the structural differences between the two states has been established only for the oxy to deoxy transition.

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Author information

Authors and Affiliations

  1. Dept. of Biochemistry and Biophysics, University of Pennsylvania and Inst. for Structural and Functional Studies, Philadelphia, PA, USA

    M. Chance, B. Chance, C. Kumar & Y. H. Chou

  2. AT&T Bell Laboratories, Murray Hill, NJ, USA

    L. Powers

  3. Dept. of Chemistry, University of Nebraska, Lincoln, NE, USA

    L. Parkhurst

Authors
  1. M. Chance
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  2. B. Chance
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  3. L. Powers
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  4. L. Parkhurst
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  5. C. Kumar
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  6. Y. H. Chou
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Editor information

Editors and Affiliations

  1. Princeton University, Princeton, New Jersey, 08544, USA

    Robert Austin

  2. B.F. Goodrich Co., Brecksville, Ohio, 44141, USA

    Ephraim Buhks

  3. University of Pennsylvania, Philadelphia, Pennsylvania, 19104, USA

    Britton Chance  & Paul Leslie Dutton  & 

  4. University of Illinois, Urbana, Illinois, 61807, USA

    Don De Vault  & Hans Frauenfelder  & 

  5. Academy of Sciences of the USSR, Moscow, USSR

    Vitalli I. Gol’danskii

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© 1987 Springer Science+Business Media New York

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Chance, M., Chance, B., Powers, L., Parkhurst, L., Kumar, C., Chou, Y.H. (1987). Structural Differences Between Rate States of Carboxyhemoglobin Compounds. In: Austin, R., et al. Protein Structure. Proceedings in Life Sciences. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-4796-8_34

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  • DOI: https://doi.org/10.1007/978-1-4612-4796-8_34

  • Publisher Name: Springer, New York, NY

  • Print ISBN: 978-1-4612-9159-6

  • Online ISBN: 978-1-4612-4796-8

  • eBook Packages: Springer Book Archive

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