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Structural analysis of the N‐ and C‐termini in a peptide with consensus sequence
Author(s) -
Gong Youxiang,
Zhou Hongxing X.,
Guo Mingming,
Kallenbach Neville R.
Publication year - 1995
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560040802
Subject(s) - linker , peptide , peptide sequence , sequence (biology) , chemistry , crystallography , c terminus , two dimensional nuclear magnetic resonance spectroscopy , stereochemistry , n terminus , protein structure , protein secondary structure , molecule , amino acid , biochemistry , computer science , organic chemistry , gene , operating system
We present a structural analysis of a peptide, the sequence of which includes amino acids that show preferences for specific positions near the N‐ and C‐termini in protein helices. This peptide has the sequence ac‐YMSEDELKAAEAAFKRHGVP‐amide, which includes a strong version of an N‐terminal Harper‐Rose capping box structure as well as a Gly located close to the C‐terminus designed to elucidate its role in C‐terminal capping. The sequence of five residues at the middle is inserted to separate effects at the two ends via a helix‐stabilizing linker. Application of a simulated annealing procedure using interproton distance constraints derived from 1 H NOESY experiments in water reveals the presence of a C‐terminal structure in this model. The C‐terminus forms a folded back structure in a significant fraction of structures generated by the annealing, in most of which Gly assumes an α L conformation. This structure occurs within a highly flexible region of the molecule and hence is occupied only a fraction of the time.