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Theoretical studies of hemoproteins. II. Dynamical behaviour of ligand binding of allosteric proteins

โœ Scribed by Takeshi Kikuchi; Kichisuke Nishimoto

Publisher
Elsevier Science
Year
1982
Tongue
English
Weight
599 KB
Volume
97
Category
Article
ISSN
0022-5193

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๐Ÿ“œ SIMILAR VOLUMES

Theoretical studies of hemoproteins. I.
Theoretical studies of hemoproteins. I. Mathematical description of the allosteric effect
โœ Takeshi Kikuchi; Kichisuke Nishimoto ๐Ÿ“‚ Article ๐Ÿ“… 1979 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 306 KB

## Abstract A new theoretical approach to the cooperativity of an enzyme has been proposed. When we applied the present theory to the allosteric effect of hemoglobin, we obtained a soโ€called Koshlandโ€“Nemethyโ€“Filmer formula. Our theory suggested that the sigmoid curve becomes sharper when the affini

Study of protein-ligand binding by fluor
Study of protein-ligand binding by fluorescence
โœ Matรญas Mรถller; Ana Denicola ๐Ÿ“‚ Article ๐Ÿ“… 2002 ๐Ÿ› The American Society for Biochemistry and Molecula ๐ŸŒ English โš– 88 KB ๐Ÿ‘ 2 views

## Abstract A practical class experiment is described to show the students an application of fluorescence spectroscopy in the study of proteinโ€ligand binding. This class is part of an undergraduate physical biochemistry course for life science students. The major aim is to introduce the students to

Effect of ligand binding on the intramin
Effect of ligand binding on the intraminimum dynamics of proteins
โœ Burak Alakent; Sena Baskan; Pemra Doruker ๐Ÿ“‚ Article ๐Ÿ“… 2010 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 876 KB

## Abstract Effects of ligand binding on protein dynamics are studied via molecular dynamics (MD) simulations on two different enzymes, dihydrofolate reductase (DHFR) and triosephosphate isomerase (TIM), in their unliganded (free) and liganded states. Domain motions in MD trajectories are analyzed