2N6I

NMR structure for a 2-stranded parallel beta-sheet

2N6I の概要

• エントリーDOI: 10.2210/pdb2n6i/pdb
• 関連するPDBエントリー: 2N4N 2N6H
• NMR情報: BMRB: 25765
• 分子名称: designed 2-stranded parallel beta-sheet (1 entity in total)
• 機能のキーワード: de novo protein
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 1728.09

構造登録者

Kung, V.M.,Cornilescu, G.,Gellman, S.H. (登録日: 2015-08-20, 公開日: 2015-10-28, 最終更新日: 2024-11-06)

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

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

実験手法

SOLUTION NMR