About: Statistical interpretation of enthalpy

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scientific article published in Nature

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rdf:type	Item
description	artículu científicu (ast) wetenschappelijk artikel (nl) article publié dans la revue scientifique Nature (fr) scientific article published in Nature (en) im Juni 1976 veröffentlichter wissenschaftlicher Artikel (de) наукова стаття, опублікована в Nature в червні 1976 (uk)
publication date	wds:Q59096083-9066B776-7121-4B1C-A8E1-61DBF9460448
publication date	1976-06-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q59096083-BF985535-E758-45BC-8757-9A9893A1A510
language of work or name	English
exact match	wds:Q59096083-72CAF092-E85C-4A36-B8E6-B25D7C449F09
exact match	https://scigraph.springernature.com/pub.10.1038/261566a0
cites work	wds:Q59096083-1BA3AD8A-476A-4C62-B5AD-B29D310E59D3 wds:Q59096083-61840B57-9A35-4B77-A3E1-5EC8F4DCEDB1 wds:Q59096083-BC19391F-5D3A-4EFC-9FDB-28B0CCE83B7D wds:Q59096083-F5072949-4146-4EF4-A2DC-B7C2A05C832F
cites work	Enthalpy-entropy compensation phenomena in water solutions of proteins and small molecules: A ubiquitous properly of water Concerning the Isokinetic Relationship Concerning the Isokinetic Relationship Determination of the Isokinetic Temperature
author name string	wds:Q59096083-746B4D7E-7F01-4DC6-ACF2-C2F99EE9F9BE wds:Q59096083-7E603C50-9F3E-47CA-A832-D7A396AE054D wds:Q59096083-AA4CCB2C-1062-4D48-A1A9-D9A02277651E
author name string	R. A. GRIEGER R. R. KRUG W. G. HUNTER
rdfs:label	Statistical interpretation of enthalpy–entropy compensation (en) Statistical interpretation of enthalpy–entropy compensation (nl)
skos:prefLabel	Statistical interpretation of enthalpy–entropy compensation (en) Statistical interpretation of enthalpy–entropy compensation (nl)
name	Statistical interpretation of enthalpy–entropy compensation (en) Statistical interpretation of enthalpy–entropy compensation (nl)
title	wds:Q59096083-214DE22E-7258-4002-BC33-1ABB55666528
title	Statistical interpretation of enthalpy–entropy compensation (en)
page(s)	wds:Q59096083-8DD8E989-A9CD-4E6B-A90D-01DB416F6437
page(s)	566-567
instance of	wds:Q59096083-CF2797ED-21BE-41DA-B4C3-93A1BE287AE7
instance of	scholarly article
main subject	wds:Q59096083-38AFEF60-7FD3-4848-85B1-8A7295D84714
main subject	statistics
published in	wds:Q59096083-2B26FE07-B7C4-4AB6-9F55-8075FF794C99
published in	Nature
issue	wds:Q59096083-9DC5DAE6-38E5-4988-8113-633903CF10B4
volume	wds:Q59096083-5EFC525D-8E48-4B82-BE63-8170D2E698C9
issue	5561
volume	261
DOI	wds:Q59096083-2390433A-6EA0-4081-BEBD-F105D3CC1EFC
DOI	http://dx.doi.org/10.1038/261566A0
DOI	10.1038/261566A0
Dimensions Publication ID	wds:Q59096083-D9D90658-9AE4-4770-A8CC-AC92E582186A
Dimensions Publication ID	1034526878
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q59096083
is cites work of	Binding Affinities of Host–Guest, Protein–Ligand, and Protein–Transition‐State Complexes Is it the shape of the cavity, or the shape of the water in the cavity? A comprehensive library of blocked dipeptides reveals intrinsic backbone conformational propensities of unfolded proteins A study on the enthalpy-entropy compensation in protein unfolding Entropy-enthalpy transduction caused by conformational shifts can obscure the forces driving protein-ligand binding The Fundamental Role of Flexibility on the Strength of Molecular Binding Entropy-enthalpy Compensation of Biomolecular Systems in Aqueous Phase: a Dry Perspective Extent of enthalpy-entropy compensation in protein-ligand interactions. Differences between retentions of various classes of aromatic hydrocarbons in reversed-phase high-performance liquid chromatography. Implications of using retention data for characterizing hydrophobicity Grid inhomogeneous solvation theory: hydration structure and thermodynamics of the miniature receptor cucurbit[7]uril Can thermodynamic measurements of receptor binding yield information on drug affinity and efficacy? Binding thermodynamics at the human neuronal nicotine receptor. Mechanistic insights into temperature-dependent regulation of the simple cyanobacterial hsp17 RNA thermometer at base-pair resolution A biochromatographic framework to evaluate the calcium effect on the antihypertensive molecule-human serum albumin binding Receptor binding thermodynamics as a tool for linking drug efficacy and affinity. Polyvalent Catalysts Operating on Polyvalent Substrates: A Model for Surface-Controlled Reactivity. Role of the Na+ ion on phenol derivatives/hydroxypropyl-beta-cyclodextrin complex formation on porous graphitic carbon phase Insights into Protein-Ligand Interactions: Mechanisms, Models, and Methods Apparent thermodynamic parameters of ligand binding to the cloned rat mu-opioid receptor Enthalpy-entropy relationship in drug-cholinoceptor interaction: a new approach Solubility behavior of barbituric acids in aqueous solution of sodium alkyl sulfonate as a function of concentration and temperature Enthalpy-entropy compensation of atomic diffusion originates from softening of low frequency phonons Size as a parameter for solvent effects on Candida antarctica lipase B enantioselectivity Investigating homology between proteins using energetic profiles Thermodynamics of heterotropic interactions. The glutamate dehydrogenase . NADPH . glutamate complex (Extra)thermodynamics of the drug-receptor interaction Triazine-human serum albumin association: thermodynamic approach and sodium effect Single Quality Factor for Enthalpy-Entropy Compensation, Iso-equilibrium and Isokinetic Relationships The microscopic structure of cold aqueous methanol mixtures. Entropy and Polarity Control the Partition and Transportation of Drug-like Molecules in Biological Membrane. Near-exact enthalpy-entropy compensation governs the thermal unfolding of protonation states of oxidized cytochrome c. Study of the Molecular Mobility in Polymers with the Thermally Stimulated Recovery Technique—A Review Thermodynamic Profiling of Carbonic Anhydrase Inhibitors
is cites work of	wds:Q34081847-85221225-C80F-44D0-9563-BE09F3C84534 wds:Q44035922-0D26CEC9-065E-4873-B5B3-FD780C67D662 wds:Q41503963-8B2D1EFE-3A5E-48CE-8F58-FEB474900937 wds:Q72912611-F85930F2-58F5-4ADF-AB72-7A937D062261 wds:Q98280930-8D16F5D9-5A4D-4D04-A41C-1F24CEC4E4D9 wds:Q37106733-BE5C1224-B81F-4E48-B56B-A290AF43DF95 wds:Q48219688-0455603B-6483-4624-84EC-755741282268 wds:Q96646320-AE7541FF-3F83-4684-8299-0365A1D68AF9 wds:Q28387381-1EB1F8E3-E85C-4A09-BC91-6E1564B1EE94 wds:Q30944043-00FD945B-EDAA-4C81-ACDF-7406FC0444A0 wds:Q26773062-7AC89CEF-B657-424B-A93F-704ACA20E6E8 wds:Q34120063-B8C4E42C-CF6C-4A6A-9BB9-6EC830772C0B wds:Q44350070-F34BE021-CC72-4458-8A04-950C7E1B77E8 wds:Q54437826-94E7EF02-60AA-47E9-8750-DDE62B99E6EC

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