(Q27683691)

1

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Nader N Nasief

2

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Michael Betz

3

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Andreas Heine

4

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David Hangauer

Angewandte Chemie International Edition

5

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language of work or name

English

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publication date

4 February 2013

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published in

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volume

52

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issue

6

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page(s)

1822-8

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cites work

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The structural dependence of amino acid hydrophobicity parameters

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Designing ligands to bind proteins

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Thermodynamics of binding of 2-methoxy-3-isopropylpyrazine and 2-methoxy-3-isobutylpyrazine to the major urinary protein

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Water, water everywhere--except where it matters?

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Mechanism of the hydrophobic effect in the biomolecular recognition of arylsulfonamides by carbonic anhydrase

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Ligand binding stepwise disrupts water network in thrombin: enthalpic and entropic changes reveal classical hydrophobic effect

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Enthalpy-entropy compensations in drug-DNA binding studies

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Motifs for molecular recognition exploiting hydrophobic enclosure in protein-ligand binding

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Native carboxypeptidase A in a new crystal environment reveals a different conformation of the important tyrosine 248

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Slow- and fast-binding inhibitors of thermolysin display different modes of binding: crystallographic analysis of extended phosphonamidate transition-state analogues

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Crystallographic structural analysis of phosphoramidates as inhibitors and transition-state analogs of thermolysin

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Phosphonamidates as transition-state analogue inhibitors of thermolysin.

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Crystal structures of alpha-mercaptoacyldipeptides in the thermolysin active site: structural parameters for a Zn monodentation or bidentation in metalloendopeptidases

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Inhibition of thermolysin and human alpha-thrombin by cobalt(III) Schiff base complexes

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An interactive computer graphics study of thermolysin-catalyzed peptide cleavage and inhibition by N-carboxymethyl dipeptides

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Experimental and computational mapping of the binding surface of a crystalline protein

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Experimental and computational active site mapping as a starting point to fragment-based lead discovery

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Fragment-based lead discovery: screening and optimizing fragments for thermolysin inhibition

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Structure of thermolysin refined at 1.6 A resolution

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Water makes the difference: rearrangement of water solvation layer triggers non-additivity of functional group contributions in protein-ligand binding

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Water mediated ligand functional group cooperativity: the contribution of a methyl group to binding affinity is enhanced by a COO(-) group through changes in the structure and thermodynamics of the hydration waters of ligand-thermolysin complexes

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Methyl effects on protein-ligand binding

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Orthogonal multipolar interactions in structural chemistry and biology

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IsoStar: a library of information about nonbonded interactions

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Water-protein interactions from high-resolution protein crystallography

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Rational approaches to improving selectivity in drug design

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