PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 8648632-0 1996 Main-chain dynamics of a partially folded protein: 15N NMR relaxation measurements of hen egg white lysozyme denatured in trifluoroethanol. Trifluoroethanol 122-138 lysozyme Homo sapiens 100-108 9369236-0 1997 Trifluoroethanol-induced conformational transition of hen egg-white lysozyme studied by small-angle X-ray scattering. Trifluoroethanol 0-16 lysozyme Homo sapiens 68-76 9369236-1 1997 The trifluoroethanol (TFE)-induced conformational transition of hen lysozyme was studied with the combined use of far-UV circular dichroism (CD) and small-angle X-ray scattering. Trifluoroethanol 4-20 lysozyme Homo sapiens 68-76 9369236-1 1997 The trifluoroethanol (TFE)-induced conformational transition of hen lysozyme was studied with the combined use of far-UV circular dichroism (CD) and small-angle X-ray scattering. Trifluoroethanol 22-25 lysozyme Homo sapiens 68-76 9369236-2 1997 At pH 2.0 and 20 degrees C, the addition of TFE to the native lysozyme induced a cooperative transition to an intermediate state with an increased helical content (TFE state). Trifluoroethanol 44-47 lysozyme Homo sapiens 62-70 9369236-2 1997 At pH 2.0 and 20 degrees C, the addition of TFE to the native lysozyme induced a cooperative transition to an intermediate state with an increased helical content (TFE state). Trifluoroethanol 164-167 lysozyme Homo sapiens 62-70 8648632-1 1996 15N NMR relaxation measurements have been used to study the dynamic behaviour of the main-chain of hen lysozyme in a partially folded state, formed in a 70% (v/v) trifluoroethanol (TFE)/30% water mixture at 37 degrees C and pH 2. Trifluoroethanol 163-179 lysozyme Homo sapiens 103-111 8648632-1 1996 15N NMR relaxation measurements have been used to study the dynamic behaviour of the main-chain of hen lysozyme in a partially folded state, formed in a 70% (v/v) trifluoroethanol (TFE)/30% water mixture at 37 degrees C and pH 2. Trifluoroethanol 181-184 lysozyme Homo sapiens 103-111 8648632-4 1996 The results imply that the dynamics of lysozyme in TFE can, at least for the great majority of residues, be adequately described by internal motions which are superimposed on all overall isotropic tumbling of the molecule. Trifluoroethanol 51-54 lysozyme Homo sapiens 39-47 8422374-0 1993 A partially folded state of hen egg white lysozyme in trifluoroethanol: structural characterization and implications for protein folding. Trifluoroethanol 54-70 lysozyme Homo sapiens 42-50 8422374-1 1993 The effect of 2,2,2-trifluoroethanol (TFE) on the solution conformation of hen egg white lysozyme has been investigated using circular dichroism (CD) and 1H nuclear magnetic resonance (NMR) spectroscopy. Trifluoroethanol 14-36 lysozyme Homo sapiens 89-97 8422374-1 1993 The effect of 2,2,2-trifluoroethanol (TFE) on the solution conformation of hen egg white lysozyme has been investigated using circular dichroism (CD) and 1H nuclear magnetic resonance (NMR) spectroscopy. Trifluoroethanol 38-41 lysozyme Homo sapiens 89-97 8422374-2 1993 Addition of TFE to lysozyme at pH 2.0, 27 degrees C, up to a concentration of 15% (v/v) induces only slight changes in the NMR spectrum. Trifluoroethanol 12-15 lysozyme Homo sapiens 19-27 18638578-1 2008 Kinetics of tertiary conformation of lysozyme adsorbed on 90 nm silica nanoparticles was inferred using tryptophan fluorescence for different surface concentrations (0.24 to 0.92 mg/m(2)), pH (4, 7 and 9), ionic strength (10 and 100 mM), 2,2,2-trifluoroethanol (TFE) (5, 15 and 30%) and Dithiothreitol (DTT) (0.5 mg/ml) concentrations. Trifluoroethanol 238-260 lysozyme Homo sapiens 37-45 18638578-1 2008 Kinetics of tertiary conformation of lysozyme adsorbed on 90 nm silica nanoparticles was inferred using tryptophan fluorescence for different surface concentrations (0.24 to 0.92 mg/m(2)), pH (4, 7 and 9), ionic strength (10 and 100 mM), 2,2,2-trifluoroethanol (TFE) (5, 15 and 30%) and Dithiothreitol (DTT) (0.5 mg/ml) concentrations. Trifluoroethanol 262-265 lysozyme Homo sapiens 37-45 14967244-4 2004 For the monohydric alcohols used in this study (methanol, ethanol, 1-propanol, n-butanol, iso-butanol and trifluoroethanol), B22 for lysozyme reaches a common plateau at approximately 5% (v/v) alcohol, while glycerol increases B22 more than monohydric alcohols. Trifluoroethanol 106-122 lysozyme Homo sapiens 133-141 14741343-0 2004 Oxidative refolding of lysozyme in trifluoroethanol (TFE) and ethylene glycol: interfering role of preexisting alpha-helical structure and intermolecular hydrophobic interactions. Trifluoroethanol 35-51 lysozyme Homo sapiens 23-31 14741343-0 2004 Oxidative refolding of lysozyme in trifluoroethanol (TFE) and ethylene glycol: interfering role of preexisting alpha-helical structure and intermolecular hydrophobic interactions. Trifluoroethanol 53-56 lysozyme Homo sapiens 23-31 14741343-1 2004 The oxidative refolding of equilibrium intermediates of lysozyme stabilized in trifluoroethanol (TFE) and ethylene glycol was monitored. Trifluoroethanol 79-95 lysozyme Homo sapiens 56-64 14741343-1 2004 The oxidative refolding of equilibrium intermediates of lysozyme stabilized in trifluoroethanol (TFE) and ethylene glycol was monitored. Trifluoroethanol 97-100 lysozyme Homo sapiens 56-64 14741343-2 2004 Equilibrium intermediates of disulfide reduced lysozyme in TFE are known to contain considerable amounts of alpha-helical structure and resemble the early intermediate in the oxidative refolding of lysozyme. Trifluoroethanol 59-62 lysozyme Homo sapiens 47-55 14741343-2 2004 Equilibrium intermediates of disulfide reduced lysozyme in TFE are known to contain considerable amounts of alpha-helical structure and resemble the early intermediate in the oxidative refolding of lysozyme. Trifluoroethanol 59-62 lysozyme Homo sapiens 198-206 7629034-6 1995 Since the inactivation of lysozyme was caused by multiple chemical reactions such as the deamidation and racemization, it was expected that the inactivation of lysozyme could be prevented by the addition of salts or TFE. Trifluoroethanol 216-219 lysozyme Homo sapiens 26-34 7629034-6 1995 Since the inactivation of lysozyme was caused by multiple chemical reactions such as the deamidation and racemization, it was expected that the inactivation of lysozyme could be prevented by the addition of salts or TFE. Trifluoroethanol 216-219 lysozyme Homo sapiens 160-168 7629034-7 1995 Thus, it was confirmed that salts and TFE suppressed the lysozyme inactivation at pH 6 and 100 degrees C. Trifluoroethanol 38-41 lysozyme Homo sapiens 57-65 34369530-2 2021 In this study, we investigate how the secondary structures of two diverse proteins - lysozyme and beta-lactoglobulin - change in the aqueous mixtures of two alcohols - ethanol and 2,2,2-trifluoroethanol (TFE) using circular dichroism measurements. Trifluoroethanol 180-202 lysozyme Homo sapiens 85-93 34369530-2 2021 In this study, we investigate how the secondary structures of two diverse proteins - lysozyme and beta-lactoglobulin - change in the aqueous mixtures of two alcohols - ethanol and 2,2,2-trifluoroethanol (TFE) using circular dichroism measurements. Trifluoroethanol 204-207 lysozyme Homo sapiens 85-93