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Biophysical Journal 57: 911-921 (1990)
© 1990 the Biophysical Society

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Statistical distribution of hydrophobic residues along the length of protein chains. Implications for protein folding and evolution.

S H White and R E Jacobs

Department of Physiology and Biophysics, University of California, Irvine 92717.

ABSTRACT

We consider in this paper the statistical distribution of hydrophobic residues along the length of protein chains. For this purpose we used a binary hydrophobicity scale which assigns hydrophobic residues a value of one and non-hydrophobes a value of zero. The resulting binary sequences are tested for randomness using the standard run test. For the majority of the 5,247 proteins examined, the distribution of hydrophobic residues along a sequence cannot be distinguished from that expected for a random distribution. This suggests that (a) functional proteins may have originated from random sequences, (b) the folding of proteins into compact structures may be much more permissive with less sequence specificity than previously thought, and (c) the clusters of hydrophobic residues along chains which are revealed by hydrophobicity plots are a natural consequence of a random distribution and can be conveniently described by binomial statistics.




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