Not all empty MHC class I molecules are molten globules: Tryptophan fluorescence reveals a two-step mechanism of thermal denaturation

Molecular Immunology

Volumn 54, Issue 3-4, 2013, Pages 386-396

  Saini, Sunil Kumar ^a   Abualrous, Esam Tolba ^a   Tigan, Anca Sarmiza ^a   Covella, Kathryn ^a   Wellbrock, Ursula ^a   Springer, Sebastian ^a  

^a JACOBS UNIVERSITY BREMEN   (Germany)

Author keywords

Ligand binding kinetics; Major histocompatibility complex class I molecules; Protein folding; Protein glycosylation; Thermal denaturation; Tryptophan fluorescence

Indexed keywords

MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; TRYPTOPHAN;

ALLOTYPE; ARTICLE; BINDING AFFINITY; ENTHALPY; ENTROPY; FLUORESCENCE ANALYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY; THERMOSTABILITY;

ANIMALS; FLUORESCENCE; GENES, MHC CLASS I; H-2 ANTIGENS; MICE; PEPTIDES; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN FOLDING; TRYPTOPHAN;

EID: 84873305369     PISSN: 01615890     EISSN: 18729142     Source Type: Journal    
DOI: 10.1016/j.molimm.2013.01.004     Document Type: Article

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