Determination de la structure primaire de la proteine du virus de la mosaïque de la luzerne (souche s) I. Determination du poids moleculaire de la proteine, de sa composition en acides amines, et utude de ses extremites net C-terminales

Two different lipid-associating domains have been identified in the B fragment of diphtheria toxin using automated Edman degradation of its cyanogen bromide peptides, secondary structure prediction analysis, and comparisons with known phospholipid-interacting proteins .The first domain is located in the highly hydrophilic (polarity index [PI] = 61 .0%) 9,000-dalton Nterminal region of fragment B . This region shows primary and predicted secondary structures dramatically similar to those found for the phospholipid headgroup-binding domains of human apolípoprotein A1 (surface lipid-associating domain) .The second domain is located in the highly hydrophobic (PI = 32.4%) middle region of fragment B . Its structure resembles that found for the membranous domain of intrinsic membrane proteins (transverse lipid-associating domain) .In contrast, the hydrophilic C-terminal 8,000-dalton region of fragment B (PI = 53 .8%) does not show structural similarity with lipid-associating domains .

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Determination de la structure primaire de la proteine du virus de la mosaïque de la luzerne (souche s) I. Determination du poids moleculaire de la proteine, de sa composition en acides amines, et utude de ses extremites net C-terminales

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References 18 publications

Primary structure of the southern bean mosaic virus coat protein: First results

Primary structure of the southern bean mosaic virus coat protein: First results

Primary structure of diphtheria toxin fragment B: structural similarities with lipid-binding domains.

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