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Structural Dynamics and Reactivity in Hemoglobin

  • Chapter
Protein Structure

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

Abstract

Proteins are macromolecular machines. In cases where the reactive centers are relatively small chromophoric units embedded in a protein matrix, they bear a resemblance to more familiar condensed phase materials such are organic mixed crystals or impurity centers in a lattice. Unlike these systems, the protein matrix has a structure that has been fine tuned over the course of evolution for a specific biological function. A major goal of biological research has been to understand how energy is both stored and utilized within these structures for the purpose of biological function. Despite the remarkable success of structural chemists and biochemists in determining the equilibrium structures and the functional properties of many protein, this problem has not been answered on a microscopic level. A major deficiency of this approach is the absence of information on how structural dynamics relates to reactivity. As a case in point, the status structure and functional properties of hemoglobin (Hb) are exceedingly well characterized [1-2], yet even for this well-studied system a detailed microscopic account of the relation between structure and function is lacking. Part of the problem is that, although high-resolution x-ray crystallographic techniques provide detailed information about equilibrium structures, they cannot be readily used to probe the transient structures that link the initial and final functional states of a protein. In recent years significant progress has been made in addressing such problems through the applications of a variety of laser based time resolved spectroscopies. At least in part these advances are the result of a chemical physics perspective based on the analogy with the impurity centers or the organic mixed crystal.

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Authors and Affiliations

  1. AT&T Bell Laboratories, Murray Hill, NJ, 07974, USA

    J. Friedman & B. Campbell

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  1. J. Friedman
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  2. B. Campbell
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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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Friedman, J., Campbell, B. (1987). Structural Dynamics and Reactivity in Hemoglobin. 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_14

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  • DOI: https://doi.org/10.1007/978-1-4612-4796-8_14

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