C. K. Engel

Toward the bilayer proteome, electrospray ionization-mass spectrometry of large, intact transmembrane proteins

Whitelegge, J. P., Le Coutre, J., Lee, J. C., Engel, C. K., Privé, G. G., Faull, K. F., ...

Genes encoding membrane proteins comprise a substantial proportion of genomes sequenced to date, but ability to perform structural studies on this portion of the proteome is limited. Electrospray...

Crystal structure of enoyl-coenzyme A (CoA) hydratase at 2.5 angstroms resolution: a spiral fold defines the CoA-binding pocket.

Engel, C K, Mathieu, M, Zeelen, J P, Hiltunen, J K, Wierenga, R K

The crystal structure of rat liver mitochondrial enoyl-coenzyme A (CoA) hydratase complexed with the potent inhibitor acetoacetyl-CoA has been refined at 2.5 angstroms resolution. This enzyme...

Toward the bilayer proteome, electrospray ionization-mass spectrometry of large, intact transmembrane proteins

Whitelegge, J. P., Le Coutre, J., Lee, J. C., Engel, C. K., Privé, G. G., Faull, K. F., ...

Genes encoding membrane proteins comprise a substantial proportion of genomes sequenced to date, but ability to perform structural studies on this portion of the proteome is limited. Electrospray...

Crystal structure of enoyl-coenzyme A (CoA) hydratase at 2.5 angstroms resolution: a spiral fold defines the CoA-binding pocket.

Engel, C K, Mathieu, M, Zeelen, J P, Hiltunen, J K, Wierenga, R K

The crystal structure of rat liver mitochondrial enoyl-coenzyme A (CoA) hydratase complexed with the potent inhibitor acetoacetyl-CoA has been refined at 2.5 angstroms resolution. This enzyme...