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Chapter 1 The energetics and specificity of enzyme—substrate interactions
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title
Chapter 1 The energetics and specificity of enzyme—substrate interactions
(English)
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author
Michael I Page
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author name string
Michael I. Page
series ordinal
1
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publication date
1984
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page(s)
1-54
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cites work
Principles that govern the folding of protein chains
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Protein Denaturation
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Experimental studies of protein folding and unfolding
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Areas, volumes, packing and protein structure
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Similarity of three-dimensional structure between the immunoglobulin domain and the copper, zinc superoxide dismutase subunit
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The conformation properties of proteins in solution
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Energetics of Ligand Binding to Proteins
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Entropic Contributions to Rate Accelerations in Enzymic and Intramolecular Reactions and the Chelate Effect
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Entropy, Binding Energy, and Enzymic Catalysis
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The energetics of neighbouring group participation
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Transition states, standard states and enzymic catalysis
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Einfluss der Configuration auf die Wirkung der Enzyme
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Structural Studies of 1,8-Disubstituted Naphthalenes as Probes for nucleophile-electrophile interactions
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The alpha-helix dipole and the properties of proteins
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The interpretation of protein structures: Estimation of static accessibility
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Hydrophobic bonding and accessible surface area in proteins
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Theoretical studies of enzymic reactions: dielectric, electrostatic and steric stabilization of the carbonium ion in the reaction of lysozyme
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Structural basis of the activation and action of trypsin
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Binding energy and enzymic catalysis
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Evidence for a thiol reagent inhibiting choline acetyltransferase by reacting with the thiol group of coenzyme a forming a potent inhibitor
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Mechanism of action of enolase: effect of the beta-hydroxy group on the rate of dissociation of the alpha-carbon-hydrogen bond
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Cysteinyl-tRNA synthetase from Escherichia coli does not need an editing mechanism to reject serine and alanine. High binding energy of small groups in specific molecular interactions
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Interaction of the peptide bond with solvent water: a vapor phase analysis
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DOI
10.1016/S0167-7306(08)60372-5
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