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The Biochemical Journal|March 7, 1998
Selectivity of post-translational modification in biotinylated proteins: the carboxy carrier protein of the acetyl-CoA carboxylase of Escherichia coliP Reche, Y L Li, C Fuller, et al.The Biochemical Journal|January 15, 1989
Cloning, sequence analysis and over-expression of the gene for the class II fructose 1,6-bisphosphate aldolase of Escherichia coliP R Alefounder, S A Baldwin, R N Perham, et al.FEBS Letters|September 12, 2000
Heteronuclear NMR studies of the specificity of the post-translational modification of biotinyl domains by biotinyl protein ligaseP A Reche, M J Howard, R W Broadhurst, et al.Ciba Foundation Symposium|January 1, 1983
Mobility and active-site coupling in 2-oxo acid dehydrogenase complexesG C Roberts, H W Duckworth, L C Packman, et al.Protein Science : a Publication of the Protein Society|May 23, 2001
Structure of a malaria parasite antigenic determinant displayed on filamentous bacteriophage determined by NMR spectroscopy: implications for the structure of continuous peptide epitopes of proteinsM Monette, S J Opella, J Greenwood, et al.The Biochemical Journal|May 1, 1978
Studies of an acid-induced species of purple membrane from Halobacterium halobiumT A Moore, M E Edgerton, G Parr, et al.Journal of Molecular Biology|February 5, 2000
Protein-protein interaction revealed by NMR T(2) relaxation experiments: the lipoyl domain and E1 component of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilusM J Howard, H J Chauhan, G J Domingo, et al.European Journal of Biochemistry|December 3, 1999
Self-assembly and catalytic activity of the pyruvate dehydrogenase multienzyme complex from Bacillus stearothermophilusG J Domingo, H J Chauhan, I A Lessard, et al.Acta Crystallographica. Section D, Biological Crystallography|March 1, 1994
A designed mutant of the enzyme glutathione reductase shortens the crystallization time by a factor of fortyP R Mittl, A Berry, N S Scrutton, et al.The Journal of Biological Chemistry|January 15, 1989
Conformational flexibility and folding of synthetic peptides representing an interdomain segment of polypeptide chain in the pyruvate dehydrogenase multienzyme complex of Escherichia coliS E Radford, E D Laue, R N Perham, et al.Pageof 37