Journal article

P-31 NUCLEAR MAGNETIC-RESONANCE STUDIES OF THE ASSOCIATION OF BASIC-PROTEINS WITH MULTILAYERS OF DIACYL PHOSPHATIDYLSERINE

R SMITH, BA CORNELL, MA KENIRY, F SEPAROVIC

BIOCHIMICA ET BIOPHYSICA ACTA | ELSEVIER SCIENCE BV | Published : 1983

Abstract

Lysozyme, cytochrome c, poly(L-lysine), myelin basic protein and ribonuclease were used to form multilayer dispersions containing about 50% protein (by weight) with bovine brain diacyl phosphatidylserine (PS). 31P nuclear magnetic resonance shift anisotropies, spin-spin (T2) and spin-lattice (T1) relaxation times for the lipid headgroup phosphorus were measured at 36.44 MHz. At pH 7.5, lysozyme, cytochrome c, poly(L-lysine) and ribonuclease were shown to increase the chemical shift anisotropy of PS by between 12-20%. Myelin basic protein altered the shape of the phosphate resonance, suggesting the presence of two lipid components, one of which had a modified headgroup conformation. The prese..

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