The helical hydrophobic moment avoids prolines in phospholipid-binding proteins

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

Research output: Contribution to journal › Article › peer-review

8 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 Gotto, \{Antonio M.\} and Knapp, \{Roger D.\} and Massey, \{John B.\}",

year = "1986",

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T1 - The helical hydrophobic moment avoids prolines in phospholipid-binding proteins

AU - Pownall, Henry J.

AU - Gotto, Antonio M.

AU - Knapp, Roger D.

AU - Massey, John B.

PY - 1986/8/29

Y1 - 1986/8/29

N2 - 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.

AB - 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.

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U2 - 10.1016/S0006-291X(86)80099-7

DO - 10.1016/S0006-291X(86)80099-7

M3 - Article

C2 - 3767953

AN - SCOPUS:0022499432

SN - 0006-291X

VL - 139

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EP - 208

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 1

ER -

The helical hydrophobic moment avoids prolines in phospholipid-binding proteins

Abstract

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