The helical hydrophobic moment avoids prolines in phospholipid-binding proteins

Henry J. Pownall; Antonio Gotto; Roger D. Knapp; John B. Massey

doi:10.1016/S0006-291X(86)80099-7

The helical hydrophobic moment avoids prolines in phospholipid-binding proteins

Henry J. Pownall, Antonio Gotto, Roger D. Knapp, John B. Massey

Research output: Contribution to journal › Article

7 Scopus citations

Abstract

Proline residues appear to punctuate the distribution of amphiphilic phospholipid-binding regions of apolipoproteins. We have applied a quantitative test to this hypothesis and shown that the magnitude of the helical hydrophobic moment around proline residues is reduced in lipid-binding proteins and peptides.

Original language	English (US)
Pages (from-to)	202-208
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	139
Issue number	1
DOIs	https://doi.org/10.1016/S0006-291X(86)80099-7
State	Published - Aug 29 1986

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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title = "The helical hydrophobic moment avoids prolines in phospholipid-binding proteins",

abstract = "Proline residues appear to punctuate the distribution of amphiphilic phospholipid-binding regions of apolipoproteins. We have applied a quantitative test to this hypothesis and shown that the magnitude of the helical hydrophobic moment around proline residues is reduced in lipid-binding proteins and peptides.",

author = "Pownall, {Henry J.} and Antonio Gotto and Knapp, {Roger D.} and Massey, {John B.}",

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