Cardiff University | Prifysgol Caerdydd ORCA
Online Research @ Cardiff 
WelshClear Cookie - decide language by browser settings

Thermal stability of heterotrimeric pMHC proteins as determined by circular dichroism spectroscopy

Fuller, Anna, Wall, Aaron, Crowther, Michael D., Lloyd, Angharad, Zhurov, Alexei ORCID: https://orcid.org/0000-0002-5594-0740, Sewell, Andrew K. ORCID: https://orcid.org/0000-0003-3194-3135, Cole, David K. ORCID: https://orcid.org/0000-0003-0028-9396 and Beck, Konrad ORCID: https://orcid.org/0000-0001-5098-9484 2017. Thermal stability of heterotrimeric pMHC proteins as determined by circular dichroism spectroscopy. Bio-protocol 7 (13) , -. 10.21769/BioProtoc.2366

[thumbnail of Bio-Protocol_PMC5524174.pdf]
Preview
PDF - Published Version
Download (1MB) | Preview
[thumbnail of Bio-Protocol_PMC5524174_Suppl.pdf]
Preview
PDF - Supplemental Material
Download (277kB) | Preview

Abstract

T cell receptor (TCR) recognition of foreign peptide fragments, presented by peptide major histocompatibility complex (pMHC), governs T-cell mediated protection against pathogens and cancer. Many factors govern T-cell sensitivity, including the affinity of the TCR-pMHC interaction and the stability of pMHC on the surface of antigen presenting cells. These factors are particularly relevant for the peptide vaccination field, in which more stable pMHC interactions could enable more effective protection against disease. Here, we discuss a method for the determination of pMHC stability that we have used to investigate HIV immune escape, T-cell sensitivity to cancer antigens and mechanisms leading to autoimmunity.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Dentistry
Medicine
Publisher: Bio-Protocol
ISSN: 2331-8325
Date of First Compliant Deposit: 1 August 2017
Last Modified: 05 Jan 2024 08:11
URI: https://orca.cardiff.ac.uk/id/eprint/102133

Actions (repository staff only)

Edit Item Edit Item

Downloads

Downloads per month over past year

View more statistics