Jump to main content
Jump to site search
Access to RSC content Close the message box

Continue to access RSC content when you are not at your institution. Follow our step-by-step guide.


Issue 11, 2020, Issue in Progress
Previous Article Next Article

The relative stability of trpzip1 and its mutants determined by computation and experiment

Author affiliations

Abstract

Six mutants of the tryptophan zipper peptide trpzip1 have been computationally and experimentally characterized. We determine the varying roles in secondary structure stability of specific residues through a mutation assay. Four of the mutations directly effect the Trp–Trp interactions and two of the mutations target the salt bridge between Glu5 and Lys8. CD spectra and thermal unfolding are used to determine the secondary structure and stability of the mutants compared to the wildtype peptide. Adaptive steered molecular dynamics has been used to obtain the energetics of the unfolding pathways of the mutations. The hydrogen bonding patterns and side-chain interactions over the course of unfolding have also been calculated and compared to wildtype trpzip1. The key finding from this work is the importance of a stabilizing non-native salt bridge pair present in the K8L mutation.

Graphical abstract: The relative stability of trpzip1 and its mutants determined by computation and experiment

Back to tab navigation

Supplementary files

Article information


Submitted
13 10 2019
Accepted
04 2 2020
First published
12 2 2020

This article is Open Access

RSC Adv., 2020,10, 6520-6535
Article type
Paper

The relative stability of trpzip1 and its mutants determined by computation and experiment

H. R. Bureau, S. Quirk and R. Hernandez, RSC Adv., 2020, 10, 6520
DOI: 10.1039/D0RA00920B

This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. Material from this article can be used in other publications provided that the correct acknowledgement is given with the reproduced material.

Reproduced material should be attributed as follows:

  • For reproduction of material from NJC:
    [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the Centre National de la Recherche Scientifique (CNRS) and the RSC.
  • For reproduction of material from PCCP:
    [Original citation] - Published by the PCCP Owner Societies.
  • For reproduction of material from PPS:
    [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the European Society for Photobiology, the European Photochemistry Association, and RSC.
  • For reproduction of material from all other RSC journals:
    [Original citation] - Published by The Royal Society of Chemistry.

Information about reproducing material from RSC articles with different licences is available on our Permission Requests page.


Social activity

Search articles by author

Spotlight

Advertisements