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

DOI: 10.21769/BioProtoc.2366 DOI Help

Authors: Anna Fuller (Cardiff University School of Medicine) , Aaron Wall (Cardiff University School of Medicine) , Michael D. Crowther (Cardiff University School of Medicine) , Angharad Lloyd (Cardiff Cardiff University School of Medicine) , Alexei Zhurov (Cardiff University School of Dentistry) , Andrew K. Sewell (Cardiff University School of Medicine) , David Cole (Cardiff University School of Medicine) , Konrad Beck (Cardiff University School of Dentistry)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Bio-Protocol , VOL 7

State: Published (Approved)
Published: July 2017
Diamond Proposal Number(s): 12332

Open Access Open Access

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.

Subject Areas: Medicine, Biology and Bio-materials, Chemistry


Instruments: B23-Circular Dichroism

Added On: 05/10/2017 16:05

Discipline Tags:

Life Sciences & Biotech Health & Wellbeing Drug Discovery Vaccines Chemistry Biochemistry

Technical Tags:

Spectroscopy Circular Dichroism (CD)