Common principles in protein folding and antigen presentation

Shan Lu; Victor E. Reyes; Rochelle R. Torgerson; Robert A. Lew; Robert E. Humphreys

doi:10.1016/0167-7799(91)90077-U

Common principles in protein folding and antigen presentation

Shan Lu, Victor E. Reyes, Rochelle R. Torgerson, Robert A. Lew, Robert E. Humphreys

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

2 Scopus citations

Abstract

The regular recurrence of hydrophobic amino acid residues along a peptide sequence determines the formation of a longitudinal hydrophobic strip when the peptide forms an α-helix. An understanding of the ways this may effect both folding of nascent proteins and antigen presentation should facilitate vaccine and therapeutics design.

Original language	English (US)
Pages (from-to)	238-242
Number of pages	5
Journal	Trends in Biotechnology
Volume	9
Issue number	1
DOIs	https://doi.org/10.1016/0167-7799(91)90077-U
State	Published - Jan 1991
Externally published	Yes

ASJC Scopus subject areas

Biotechnology
Bioengineering

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10.1016/0167-7799(91)90077-U

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title = "Common principles in protein folding and antigen presentation",

abstract = "The regular recurrence of hydrophobic amino acid residues along a peptide sequence determines the formation of a longitudinal hydrophobic strip when the peptide forms an α-helix. An understanding of the ways this may effect both folding of nascent proteins and antigen presentation should facilitate vaccine and therapeutics design.",

author = "Shan Lu and Reyes, {Victor E.} and Torgerson, {Rochelle R.} and Lew, {Robert A.} and Humphreys, {Robert E.}",

year = "1991",

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doi = "10.1016/0167-7799(91)90077-U",

language = "English (US)",

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journal = "Trends in Biotechnology",

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AU - Lu, Shan

AU - Reyes, Victor E.

AU - Torgerson, Rochelle R.

AU - Lew, Robert A.

AU - Humphreys, Robert E.

PY - 1991/1

Y1 - 1991/1

N2 - The regular recurrence of hydrophobic amino acid residues along a peptide sequence determines the formation of a longitudinal hydrophobic strip when the peptide forms an α-helix. An understanding of the ways this may effect both folding of nascent proteins and antigen presentation should facilitate vaccine and therapeutics design.

AB - The regular recurrence of hydrophobic amino acid residues along a peptide sequence determines the formation of a longitudinal hydrophobic strip when the peptide forms an α-helix. An understanding of the ways this may effect both folding of nascent proteins and antigen presentation should facilitate vaccine and therapeutics design.

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U2 - 10.1016/0167-7799(91)90077-U

DO - 10.1016/0167-7799(91)90077-U

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AN - SCOPUS:0025815965

SN - 0167-7799

VL - 9

SP - 238

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JO - Trends in Biotechnology

JF - Trends in Biotechnology

IS - 1

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Common principles in protein folding and antigen presentation

Abstract

ASJC Scopus subject areas

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