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New Ways to Look at Old Proteins

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Methods in Protein Sequence Analysis · 1986

Part of the book series: Experimental Biology and Medicine ((EBAM,volume 14))

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Abstract

Protein chemistry has evolved in stages, and like all experimental sciences, each stage was set by fundamental innovations in methodologies. The exploration of the macromolecular structure of proteins depended on several innovative methods: the ultracentrifuge and boundary electrophoresis proved that proteins had uniform molecular mass and, charge; amino acid analysis demonstrated their unique chemical compositions. Ion exchange chromatography and gel filtration, in conjunction with the fraction collector facilitated the fractionation and isolation of pure proteins and peptides. The systematic determination of protein and peptide sequences had to await the Edman method of stepwise degradation and its subsequent automation by liquid, solid or gas phase sequencers. On another front, the development of computers facilitated the application of X-ray crystallography to the determination of the three-dimensional structure of proteins.

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Authors and Affiliations

  1. Department of Biochemistry, SJ-70, University of Washington, Seattle, Washington, 98195, USA

    Hans Neurath

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  1. Hans Neurath
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Editors and Affiliations

  1. Department of Biochemistry, University of Washington, Seattle, Washington, USA

    Kenneth A. Walsh (Chairman) (Chairman)

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Neurath, H. (1987). New Ways to Look at Old Proteins. In: Walsh, K.A. (eds) Methods in Protein Sequence Analysis · 1986. Experimental Biology and Medicine, vol 14. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-59259-480-1_1

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  • DOI: https://doi.org/10.1007/978-1-59259-480-1_1

  • Publisher Name: Humana Press, Totowa, NJ

  • Print ISBN: 978-1-4757-5826-9

  • Online ISBN: 978-1-59259-480-1

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