Influence of α-Helices on the Emulsifying Properties of Proteins | Zendy

Simon Poon | Zendy; Adrienne E. Clarke | Zendy; Graeme Currie | Zendy; Carolyn J. Schultz | Zendy

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Influence of α-Helices on the Emulsifying Properties of Proteins

Author(s) -

Simon Poon,

Adrienne E. Clarke,

Graeme Currie,

Carolyn J. Schultz

Publication year - 2001

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.65.1713

Subject(s) - cyanogen bromide , peptide , chemistry , molecule , amphiphile , cleavage (geology) , sequence (biology) , hydrophobic effect , peptide sequence , stereochemistry , crystallography , biochemistry , organic chemistry , materials science , polymer , copolymer , gene , fracture (geology) , composite material

A peptide derived from apomyoglobin by cyanogen bromide cleavage was found to be an active emulsifier. This molecule, peptide 1-55, has two potential amphipathic alpha-helices and a hydrophilic C-terminal domain. The importance of each of these domains to the emulsifying properties of this molecule was investigated by testing the products of gene constructs based on the sequence of peptide 1-55, but lacking one of the three domains. The emulsifying activity of the peptides lacking either of the alpha-helices was correlated with the hydrophobic moments of their respective helices. The hydrophobic moment is a measure of the amphipathicity of alpha-helices; a hydrophobic moment analysis of other emulsifying peptides supports the hypothesis that a high hydrophobic moment contributes to good emulsifying properties in a molecule which contains alpha-helices.

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