GSBS Student Publications

Title

Prediction of alpha helices and T cell-presented sequences in proteins with algorithms based on strip-of-helix hydrophobicity index

UMMS Affiliation

Graduate School of Biomedical Sciences; Department of Pharmacology

Date

1-1-1991

Document Type

Article

Medical Subject Headings

Algorithms; Amino Acids; Antigen-Presenting Cells; Epitopes; *Forecasting; Models, Chemical; Peptides; *Protein Conformation; Proteins; T-Lymphocytes

Disciplines

Life Sciences | Medicine and Health Sciences

Abstract

Recurrent aliphatic hydrophobic amino acids which occur in the sequence of a protein or a peptide at positions which form an axial, hydrophobic strip when the sequence is coiled as an alpha helix might stabilize coiling against hydrophobic surfaces. That effect can lead to helix formation against hydrophobic cores of nascent proteins or excised T cell-presented peptides and to protease protection and scavenging for presentation by MHC molecules. Such consensus sequences of recurrent hydrophobicity creating a scavenger "S" site might overlap to varying degrees the T cell-presented "T" epitope which actually sits in the antigen-binding site of a MHC molecules, as long as a cleavage "C" site does not fall between them when they are relatively separated. Cooperatively among the residues in an axial, hydrophobic strip to stabilize helix formation is reflected in the SOHHI, which is the mean hydrophobicity of residues in such potential strips. Algorithms based on the SOHHI, with additional considerations related to length and caps, lead to sensitive and efficient predictions of structural helices and of T cell-presented epitopes. In experimental tests of these ideas, the SOHHI was found to correlate to helical coiling of amphiphilic peptides in the presence of lipid vesicles. These principles lead to hypotheses to alter the potency and range of MHC restriction of peptide vaccines or to decrease the immunogenicity of therapeutic proteins.

Rights and Permissions

Citation: Methods Enzymol. 1991;202:225-38.

Related Resources

Link to Article in PubMed

Journal Title

Methods in enzymology

PubMed ID

1723780