Abstract
Traditionally, proteins have been regarded as well-defined, uniform molecules, where one molecule is virtually identical to the next. This notion has been supported by the fact that the highly efficient protein primary structure analysis by prediction from the DNA sequence will result in a well-defined, unique amino acid sequence, containing no direct indication of any kind of modification or processing. However, information is accumulating about protein heterogeneity, co- or post-translational modification and processing as well as about the functional implications of the structural variation (Krishna and Wold, 1993; Graves et al., 1994). Human fibrinogen may serve as an extreme example of a protein existing in a multitude of structural forms, many of which have been demonstrated to differ in functional properties (Henschen and McDonagh, 1986; Henschen, 1993). In the following, the various, so far recognized structural variations and their possible function effects, together with some relevant identification procedures will be described.
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Henschen-Edman, A.H. (1995). Human Fibrinogen Occurs as Over 1 Million Non-Identical Molecules. In: Atassi, M.Z., Appella, E. (eds) Methods in Protein Structure Analysis. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1031-8_39
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DOI: https://doi.org/10.1007/978-1-4899-1031-8_39
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