Journal ArticleDOI
Magnetic resonance studies of protein-small molecule interactions. Dynamics of binding between N-trifluoroacetyl-D-tryptophan and .alpha.-chymotrypsin
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This article is published in Journal of the American Chemical Society.The article was published on 1972-06-28. It has received 24 citations till now. The article focuses on the topics: Two-dimensional nuclear magnetic resonance spectroscopy & Solid-state nuclear magnetic resonance.read more
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Journal ArticleDOI
Kinetics of subtilisin and thiolsubtilisin.
Manfred Philipp,Myron L. Bender +1 more
TL;DR: The observation that these transition state analog inhibitors bind poorly to thiol Subtilisin while other compounds bind nearly equally well to both enzymes suggests that thiolsubtilisin may not be able to stabilize the transition state during acylation by specific substrates.
Journal ArticleDOI
Binding of small molecules to proteins.
Aksel A. Bothner,R. Gassend +1 more
TL;DR: It is observed that in macromolecules a different relationship occurs that leads to new and interesting applications of the homonuclear Overhauser effect, and its power in elucidating the geometry of small molecules has been convincingly demonstrated.
Journal ArticleDOI
Mechanism of action of serine proteases: tetrahedral intermediate and concerted proton transfer.
TL;DR: Stopped-flow spectrophotometry and proton inventory experiments have been used to define the reaction pathway for hydrolysis of a specific peptide substrate by the serine proteases elastase and alpha-lytic protease, and suggest the simultaneous transfer of two protons leading to breakdown of the tetrahedral complex.
Book ChapterDOI
Protein-ligand interactions: exchange processes and determination of ligand conformation and protein-ligand contacts.
TL;DR: This chapter describes exchange processes and determination of ligand conformation and protein-ligand contacts, and dynamic, kinetic, and thermodynamic aspects of lig and binding are presented.
Book ChapterDOI
Fluorine nuclear magnetic resonance of fluorinated ligands.
TL;DR: NMR studies of fluorinated ligands in enzyme structures offer a number of operational advantages and can produce results indicative of binding stoichiometry, ionization behavior, enzyme dynamics, and conformational changes.
Related Papers (5)
Mechanism of the -chymotrypsin-catalyzed hydrolysis of amides. pH dependence of k c and K m . Kinetic detection of an intermediate.
Alan R. Fersht,Yolanda Requena +1 more