6GWX

Stabilising and Understanding a Miniprotein by Rational Design.

Summary for 6GWX

• Entry DOI: 10.2210/pdb6gwx/pdb
• Related: 5LO2
• NMR Information: BMRB: 34295
• Descriptor: Optimised PPa-TYR (1 entity in total)
• Functional Keywords: designed miniprotein ch-pi interactions weak non-covalent interactions in protiens solution structure proline-tyrosine interactions, structural protein
• Biological source: Streptococcus mutans
• Total number of polymer chains: 1
• Total formula weight: 3791.35

Authors

Porter Goff, K.L.,Williams, C.,Baker, E.G.,Nicol, D.,Samphire, J.L.,Zieleniewski, F.L.,Crump, M.P.,Woolfson, D.N. (deposition date: 2018-06-26, release date: 2019-07-10, Last modification date: 2024-11-20)

Primary citation

Porter Goff, K.L.,Nicol, D.,Williams, C.,Crump, M.P.,Zieleniewski, F.,Samphire, J.L.,Baker, E.G.,Woolfson, D.N.
Stabilizing and Understanding a Miniprotein by Rational Redesign.
Biochemistry, 58:3060-3064, 2019

PubMed Abstract: Miniproteins reduce the complexity of the protein-folding problem allowing systematic studies of contributions to protein folding and stabilization. Here, we describe the rational redesign of a miniprotein, PPα, comprising a polyproline II helix, a loop, and an α helix. The redesign provides a framework for interrogating noncovalent interactions. Optimized PPα has significantly improved thermal stability with a midpoint unfolding temperature () of 51 °C. Its nuclear magnetic resonance structure indicates a density of stabilizing noncovalent interactions that is higher than that of the parent peptide, specifically an increased number of CH-π interactions. In part, we attribute this to improved long-range electrostatic interactions between the two helical elements. We probe further sequence-stability relationships in the miniprotein through a series of rational mutations.

PubMed: 31251570
DOI: 10.1021/acs.biochem.9b00067

Experimental method

SOLUTION NMR