The paradoxical thermodynamic basis for the interaction of ethylene glycol, glycine, and sarcosine chains with bovine carbonic anhydrase II: an unexpected manifestation of enthalpy/entropy compensation.
about
Structural Analysis of Charge Discrimination in the Binding of Inhibitors to Human Carbonic Anhydrases I and IIOrigin of Heat Capacity Changes in a “Nonclassical” Hydrophobic InteractionStructural and Biochemical Characterization of the Interaction between KPC-2 β-Lactamase and β-Lactamase Inhibitor Protein,Thermodynamic optimisation in drug discovery: a case study using carbonic anhydrase inhibitorsFluoroalkyl and Alkyl Chains Have Similar Hydrophobicities in Binding to the “Hydrophobic Wall” of Carbonic AnhydraseProtein–Ligand Interactions: Thermodynamic Effects Associated with Increasing Nonpolar Surface AreaProtein–ligand interactions: Probing the energetics of a putative cation–π interactionEntropy-enthalpy transduction caused by conformational shifts can obscure the forces driving protein-ligand bindingDependence of Effective Molarity on Linker Length for an Intramolecular Protein−Ligand SystemA multidisciplinary approach to probing enthalpy-entropy compensation and the interfacial mobility model.Bridging Calorimetry and Simulation through Precise Calculations of Cucurbituril-Guest Binding Enthalpies.Ligand-induced protein mobility in complexes of carbonic anhydrase II and benzenesulfonamides with oligoglycine chainsThe Fundamental Role of Flexibility on the Strength of Molecular Binding.Designing ligands to bind proteinsConfigurational space discretization and free energy calculation in complex molecular systems.Thermodynamic parameters for the association of fluorinated benzenesulfonamides with bovine carbonic anhydrase II.Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein-ligand binding.Protein-Ligand Interactions: Thermodynamic Effects Associated with Increasing the Length of an Alkyl Chain.A medicinal chemist's guide to molecular interactionsMolecular recognition in chemical and biological systems.Denaturation of proteins by SDS and tetraalkylammonium dodecyl sulfates.Extent of enthalpy-entropy compensation in protein-ligand interactions.Dependence of avidity on linker length for a bivalent ligand-bivalent receptor model system.Thermodynamic studies of a series of homologous HIV-1 TAR RNA ligands reveal that loose binders are stronger Tat competitors than tight ones.An enthalpic basis of additivity in biphenyl hydroxamic acid ligands for stromelysin-1Water accessibility to the binding cleft as a major switching factor from entropy-driven to enthalpy-driven binding of an alkyl group by synthetic receptors.Molecular rigidity and enthalpy-entropy compensation in DNA melting.Mutations designed to destabilize the receptor-bound conformation increase MICA-NKG2D association rate and affinity.Solvent effects on ligand binding to a serine protease.Connecting Classical QSAR and LERE Analyses Using Modern Molecular Calculations, LERE-QSAR (VI): Hydrolysis of Substituted Hippuric Acid Phenyl Esters by Trypsin.The importance of hydration thermodynamics in fragment-to-lead optimization.Effects of surface charge on denaturation of bovine carbonic anhydraseHydrophobic alkyl chains substituted to the 8-position of cyclic nucleotides enhance activation of CNG and HCN channels by an intricate enthalpy - entropy compensationThermodynamic Profiling of Carbonic Anhydrase InhibitorsIs it the shape of the cavity, or the shape of the water in the cavity?
P2860
Q27644345-7885D16C-62DA-4696-A983-567C3EBE7AFDQ27646631-98E07957-E604-413B-896E-1A11C1056DF3Q27657333-5CA3314F-74CB-4F9B-8D49-33BBAB80C967Q27658036-92822D40-2011-4A87-A2CE-1396109B8BB5Q27671014-9F342A60-7BF9-4699-8780-DE536EDC8C38Q27675114-F02D5681-7855-421B-BA06-E8AB42C735C7Q27683926-3FCC399C-635E-4DAD-97C0-5CC623B3CDB7Q28392085-1E5FFB76-7676-4DF6-9A69-462C73D01656Q29038357-F9B97265-3D62-4C02-B206-12C9CB5EF6E3Q30503303-91F76812-6F47-4BFB-94F5-B3B8D332E45CQ34155663-585DD6F7-4892-4145-8F4D-B3D52FA79B24Q34614404-DCD74EB0-01B8-471E-9041-CA91F152B1EDQ36029911-2B22A027-2FA2-4ECD-9C6C-70D818DF6E78Q36526030-9E7112FD-5F8C-4083-9408-5A124C1315ACQ36683075-273521FD-6154-495F-927E-EA833B573A6AQ37069146-7FB90BB6-2CA4-40C3-ACCD-9609B7F9C25AQ37108161-FDED776C-89B5-4CDA-AA0E-0293E84D3039Q37384155-94BD846C-15FE-4569-B176-0DC47782F55BQ37719514-BD4783E1-9D2D-420F-8D86-AB33464F5969Q38335784-60454288-9366-439F-BD14-066E1D6A23AFQ38397146-3C8FAC34-A64E-4A8D-8DAC-BF5C8BDDFE45Q38666534-893BC9F6-020F-4F9A-9585-AA5A481ACF75Q40862828-745E9686-56F4-4552-983A-6AC5E8B379BFQ42010727-ADA8C219-8B24-4EA6-8EEF-ACCB41B51361Q42586127-61C23A7A-0BE2-4DEE-B191-09BB4EC472E7Q43105021-DFD521A0-AE45-40A6-B379-CB6D6D990BF6Q47422914-B42C7937-A0CC-41A2-8D91-6CC9DCF86251Q47597641-8D069A40-0FD1-4613-BBC7-47F0228AE40BQ48049114-E8176DE7-A38C-4661-983C-5525D8EB0D28Q53749950-C4DAD3D0-EDF9-4230-8815-EEE8D2B3093AQ54326694-D5487C0F-3DAD-4E4C-ADE0-9802ADEDA104Q57133014-E9A932F8-53B7-4FDF-A3E9-D00A919AC41AQ57296153-70872C62-9945-4524-92FC-7E7F1C6172AEQ58293116-F1987DE1-7342-41B2-98DD-D869F5A89605Q58483826-2591E802-444C-4329-B1C8-F7F825EECE4D
P2860
The paradoxical thermodynamic basis for the interaction of ethylene glycol, glycine, and sarcosine chains with bovine carbonic anhydrase II: an unexpected manifestation of enthalpy/entropy compensation.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
@zh
2006年论文
@zh-cn
name
The paradoxical thermodynamic ...... enthalpy/entropy compensation.
@en
type
label
The paradoxical thermodynamic ...... enthalpy/entropy compensation.
@en
prefLabel
The paradoxical thermodynamic ...... enthalpy/entropy compensation.
@en
P2093
P2860
P356
P1476
The paradoxical thermodynamic ...... enthalpy/entropy compensation.
@en
P2093
Brooks R Bohall
George M Whitesides
Vijay M Krishnamurthy
Vincent Semetey
P2860
P304
P356
10.1021/JA060070R
P407
P577
2006-05-01T00:00:00Z