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Naturstoffe pp 41–64Cite as

The Structure of Haemoglobin

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Part of the book series: Fortschritte der Chemischen Forschung ((TOPCURRCHEM,volume 6))

Abstract

Proteins are large complex molecules consisting of polymers of amino acids. In order to understand the way in which they function it is essential to have a knowledge of the geometry of their structure, that is of their three-dimensional conformation, as well as of their chemical composition. The activity of a protein may be lost by the process of denaturation (which may be reversible) in which no chemical bonds are broken but the three-dimensional conformation is altered; conversely the molecule may become active when sections, which are quite distinct chemically, are brought close to each other. Many proteins contain prosthetic groups at the site of their catalytic activity. These are non-protein groups, such as the haem group in myoglobin or haemoglobin, and the activity depends on the specific protein molecule to which they are attached. The chemical sequence of a protein molecule is genetically determined. This is demonstrated by the abnormal human haemoglobins in which abnormalities, which consist of the substitution of a single amino acid by a different one, are inherited in a Mendelian manner (12, 20). It is widely believed that the three-dimensional structure is determined by this chemical sequence; that is that it is the most energetically favourable conformation of the polypeptide chains.

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Authors and Affiliations

  1. Department of Chemistry, Harvard University Cambridge, Mass., USA

    Dr. Hilary Muirhead

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  1. Dr. Hilary Muirhead
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© 1996 Springer-Verlag Berlin Heidelberg

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Muirhead, H. (1996). The Structure of Haemoglobin. In: Naturstoffe. Fortschritte der Chemischen Forschung, vol 6. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-25280-2_2

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  • DOI: https://doi.org/10.1007/978-3-662-25280-2_2

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-662-23258-3

  • Online ISBN: 978-3-662-25280-2

  • eBook Packages: Springer Book Archive

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