cis-2-aminocyclopentanecarboxylic acid oligomers adopt a sheetlike structure

Switch from helix to nonpolar strand

Research output: Contribution to journalArticle

112 Citations (Scopus)

Abstract

Rational control over helix and strand secondary structures is possible when conformationally restricted cyclic β-amino acid residues are incorporated in the β-peptides. Inversion of the relative configuration of these residues enables the preferred periodic structure to be switched from a helix to a single nonpolar strand (see picture).

Original languageEnglish
Pages (from-to)1718-1721
Number of pages4
JournalAngewandte Chemie - International Edition
Volume41
Issue number10
DOIs
Publication statusPublished - 2002

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Cyclic Amino Acids
Cycloleucine
Periodic structures
Oligomers
Peptides
Amino acids
Switches
Acids

Keywords

  • Amino acids
  • Chirality
  • Conformation analysis
  • NMR spectroscopy
  • Peptides

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

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title = "cis-2-aminocyclopentanecarboxylic acid oligomers adopt a sheetlike structure: Switch from helix to nonpolar strand",
abstract = "Rational control over helix and strand secondary structures is possible when conformationally restricted cyclic β-amino acid residues are incorporated in the β-peptides. Inversion of the relative configuration of these residues enables the preferred periodic structure to be switched from a helix to a single nonpolar strand (see picture).",
keywords = "Amino acids, Chirality, Conformation analysis, NMR spectroscopy, Peptides",
author = "T. Martinek and G. T{\'o}th and E. Vass and M. Holl{\'o}si and F. F{\"u}l{\"o}p",
year = "2002",
doi = "10.1002/1521-3773(20020517)41:10<1718::AID-ANIE1718>3.0.CO;2-2",
language = "English",
volume = "41",
pages = "1718--1721",
journal = "Angewandte Chemie - International Edition",
issn = "1433-7851",
publisher = "John Wiley and Sons Ltd",
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}

TY - JOUR

T1 - cis-2-aminocyclopentanecarboxylic acid oligomers adopt a sheetlike structure

T2 - Switch from helix to nonpolar strand

AU - Martinek, T.

AU - Tóth, G.

AU - Vass, E.

AU - Hollósi, M.

AU - Fülöp, F.

PY - 2002

Y1 - 2002

N2 - Rational control over helix and strand secondary structures is possible when conformationally restricted cyclic β-amino acid residues are incorporated in the β-peptides. Inversion of the relative configuration of these residues enables the preferred periodic structure to be switched from a helix to a single nonpolar strand (see picture).

AB - Rational control over helix and strand secondary structures is possible when conformationally restricted cyclic β-amino acid residues are incorporated in the β-peptides. Inversion of the relative configuration of these residues enables the preferred periodic structure to be switched from a helix to a single nonpolar strand (see picture).

KW - Amino acids

KW - Chirality

KW - Conformation analysis

KW - NMR spectroscopy

KW - Peptides

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U2 - 10.1002/1521-3773(20020517)41:10<1718::AID-ANIE1718>3.0.CO;2-2

DO - 10.1002/1521-3773(20020517)41:10<1718::AID-ANIE1718>3.0.CO;2-2

M3 - Article

VL - 41

SP - 1718

EP - 1721

JO - Angewandte Chemie - International Edition

JF - Angewandte Chemie - International Edition

SN - 1433-7851

IS - 10

ER -