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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Journal of mathematical chemistry 17 (1995), S. 167-184 
    ISSN: 1572-8897
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mathematics
    Notes: Abstract The hydrophobic amino acids that make up the core of a protein can be expected to be closer together than the rest of the residues in the molecule and are likely to remain conserved during evolution due to their important role. In the present study, a general theoretical framework is provided for estimating interresidue distances from residue hydrophobicity and conservation deduced from multiple alignments. While the accurate prediction of individual distances by statistical procedures is theoretically impossible, the method is able to match the distribution of predicted distances to a prescribed distribution with good accuracy.
    Type of Medium: Electronic Resource
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