Fast association rates suggest a conformational change in the MHC class I molecule H-2Db upon peptide binding.

Springer, S; Doring, K; Skipper, JC; Townsend, AR; Cerundolo, V

Abstract:

Major histocompatibility complex (MHC) class I molecules bind peptides in the endoplasmic reticulum (ER). For this binding reaction, when performed in vitro, widely differing association rates have been reported. We have expressed empty soluble H-2Db class I molecules in Chinese hamster ovary (CHO) cells and generated complete sets of association, dissociation, and equilibrium constants of unmodified peptides using tritium-labeled peptides and stopped-flow fluorescence spectroscopy. We find t...

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APA Style

Springer, S., Doring, K., Skipper, J. C., Townsend, A. R., & Cerundolo, V. (1998). Fast association rates suggest a conformational change in the MHC class I molecule H-2Db upon peptide binding. Biochemistry, 37(9), 3001–3012.

MLA Style

Springer, S., et al. “Fast Association Rates Suggest a Conformational Change in the MHC Class I Molecule H-2Db upon Peptide Binding.” Biochemistry, vol. 37, no. 9, Biochemistry, 1998, pp. 3001–12.

Chicago Style

Springer, S, K Doring, JC Skipper, AR Townsend, and V Cerundolo. 1998. “Fast Association Rates Suggest a Conformational Change in the MHC Class I Molecule H-2Db upon Peptide Binding.” Biochemistry 37 (9): 3001–12.
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