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pro vyhledávání: '"Carol M. Porter"'
Autor:
A. Carl Whittington, Shawn M. Sternisha, Gianluigi Veglia, Malcolm M. McCray, Juliana A. Martinez Fiesco, Brian G. Miller, Carol M. Porter, Timothy M. Logan, Peter J. Steinbach, Cristina Olivieri
Publikováno v:
Biophys J
Human glucokinase (GCK) is the prototypic example of an emerging class of proteins with allosteric-like behavior that originates from intrinsic polypeptide dynamics. High-resolution NMR investigations of GCK have elucidated millisecond-timescale dyna
Publikováno v:
Protein Science. 23:915-922
Glucokinase (GCK, hexokinase IV) is a monomeric enzyme with a single glucose binding site that displays steady-state kinetic cooperativity, a functional characteristic that affords allosteric regulation of GCK activity. Structural evidence suggests t
Autor:
Brian G. Miller, Carol M. Porter
Publikováno v:
Bioorganic Chemistry. 43:44-50
Cooperativity is widespread in biology. It empowers a variety of regulatory mechanisms and impacts both the kinetic and thermodynamic properties of macromolecular systems. Traditionally, cooperativity is viewed as requiring the participation of multi
Publikováno v:
Protein science : a publication of the Protein Society. 23(7)
Glucokinase (GCK, hexokinase IV) is a monomeric enzyme with a single glucose binding site that displays steady-state kinetic cooperativity, a functional characteristic that affords allosteric regulation of GCK activity. Structural evidence suggests t