Abstract
Recent knowledge about the determinants of β-sheet formation and stability has notably been improved by the structural analysis of model peptides with β-hairpin structure in aqueous solution. Several experimental studies have shown that the turn region residues can not only determine the stability, but also the conformation of the β-hairpin. Specific interstrand side-chain interactions, hydrophobic and polar, have been found to be important stabilizing interactions. The knowledge acquired in the recent years from peptide systems, together with the information gathered from mutants in proteins, and the analysis of known protein structures, has led to successful design of a folded three-stranded monomeric β-sheet structure. Copyright (C) 1999 Elsevier Science Ltd.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 93-103 |
| Number of pages | 11 |
| Journal | Bioorganic and Medicinal Chemistry |
| Volume | 7 |
| Issue number | 1 |
| DOIs | |
| State | Published - Jan 1999 |
| Externally published | Yes |
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Keywords
- β-hairpin
- β-sheet
- NMR
- Peptides
- Protein folding
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Organic Chemistry
- Drug Discovery
- Pharmaceutical Science
Cite this
β-hairpin and β-sheet formation in designed linear peptides. / Ramirez-Alvarado, Marina; Kortemme, Tanja; Blanco, Francisco J.; Serrano, Luis.
In: Bioorganic and Medicinal Chemistry, Vol. 7, No. 1, 01.1999, p. 93-103.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - β-hairpin and β-sheet formation in designed linear peptides
AU - Ramirez-Alvarado, Marina
AU - Kortemme, Tanja
AU - Blanco, Francisco J.
AU - Serrano, Luis
PY - 1999/1
Y1 - 1999/1
N2 - Recent knowledge about the determinants of β-sheet formation and stability has notably been improved by the structural analysis of model peptides with β-hairpin structure in aqueous solution. Several experimental studies have shown that the turn region residues can not only determine the stability, but also the conformation of the β-hairpin. Specific interstrand side-chain interactions, hydrophobic and polar, have been found to be important stabilizing interactions. The knowledge acquired in the recent years from peptide systems, together with the information gathered from mutants in proteins, and the analysis of known protein structures, has led to successful design of a folded three-stranded monomeric β-sheet structure. Copyright (C) 1999 Elsevier Science Ltd.
AB - Recent knowledge about the determinants of β-sheet formation and stability has notably been improved by the structural analysis of model peptides with β-hairpin structure in aqueous solution. Several experimental studies have shown that the turn region residues can not only determine the stability, but also the conformation of the β-hairpin. Specific interstrand side-chain interactions, hydrophobic and polar, have been found to be important stabilizing interactions. The knowledge acquired in the recent years from peptide systems, together with the information gathered from mutants in proteins, and the analysis of known protein structures, has led to successful design of a folded three-stranded monomeric β-sheet structure. Copyright (C) 1999 Elsevier Science Ltd.
KW - β-hairpin
KW - β-sheet
KW - NMR
KW - Peptides
KW - Protein folding
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UR - http://www.scopus.com/inward/citedby.url?scp=0039404627&partnerID=8YFLogxK
U2 - 10.1016/S0968-0896(98)00215-6
DO - 10.1016/S0968-0896(98)00215-6
M3 - Article
C2 - 10199660
AN - SCOPUS:0039404627
VL - 7
SP - 93
EP - 103
JO - Bioorganic and Medicinal Chemistry
JF - Bioorganic and Medicinal Chemistry
SN - 0968-0896
IS - 1
ER -