PDBsum entry 2n4n

De novo protein

PDB id: 2n4n

Contents

Protein chain

25 a.a.

PDB id:

2n4n

Name:

De novo protein

Title:

Nmr structure for a 3-stranded parallel beta-sheet

Structure:

Designed beta sheet. Chain: a. Engineered: yes

Source:

Synthetic: yes. Synthetic construct. Organism_taxid: 32630

NMR struc:

10 models

Authors:

V.M.Kung,G.Cornilescu,S.H.Gellman

Key ref:

V.M.Kung et al. (2015). Impact of Strand Number on Parallel β-Sheet Stability. Angew Chem Int Ed Engl, 54, 14336-14339. PubMed id: 26457984 DOI: 10.1002/anie.201506448

Date:

24-Jun-15 Release date: 28-Oct-15

Protein chain

No UniProt id for this chain

Struc: 24 a.a.

DOI no: 10.1002/anie.201506448

Angew Chem Int Ed Engl 54:14336-14339 (2015)

PubMed id: 26457984

Impact of Strand Number on Parallel β-Sheet Stability.

V.M.Kung, G.Cornilescu, S.H.Gellman.

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.