Loading
PDBj
メニューPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2N4N

NMR structure for a 3-stranded parallel beta-sheet

2N4N の概要
エントリーDOI10.2210/pdb2n4n/pdb
NMR情報BMRB: 25673
分子名称DESIGNED BETA SHEET (1 entity in total)
機能のキーワードde novo protein
由来する生物種synthetic construct
タンパク質・核酸の鎖数1
化学式量合計2877.45
構造登録者
Kung, V.M.,Cornilescu, G.,Gellman, S.H. (登録日: 2015-06-24, 公開日: 2015-10-28, 最終更新日: 2024-11-27)
主引用文献Kung, V.M.,Cornilescu, G.,Gellman, S.H.
Impact of Strand Number on Parallel beta-Sheet Stability.
Angew.Chem.Int.Ed.Engl., 54:14336-14339, 2015
Cited by
PubMed Abstract: We have examined whether parallel β-sheet secondary structure becomes more stable as the number of β-strands increases, via comparisons among peptides designed to adopt two- or three-stranded parallel β-sheet conformations in aqueous solution. Our three-strand design is the first experimental model of a triple-stranded parallel β-sheet. Analysis of the designed peptides by nuclear magnetic resonance (NMR) and circular dichroism (CD) spectroscopy supports the hypothesis that increasing the number of β-strands, from two to three, increases the stability of the parallel β-sheet. We present the first experimental evidence for cooperativity in the folding of a triple-stranded parallel β-sheet, and we show how minimal model systems may enable experimental documentation of characteristic properties, such as CD spectra, of parallel β-sheets.
PubMed: 26457984
DOI: 10.1002/anie.201506448
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 2n4n
検証レポート(詳細版)ダウンロードをダウンロード

248636

件を2026-02-04に公開中

PDB statisticsPDBj update infoContact PDBjnumon