PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 19629659-6 2009 Myoglobin was dissolved in pure methanol, ethylene glycol and glycerol. Glycerol 62-70 myoglobin Homo sapiens 0-9 21425816-1 2011 For the first time, a systematic investigation of the glass transition and its related dynamics of myoglobin in water-glycerol solvent mixtures of different water contents is presented. Glycerol 118-126 myoglobin Homo sapiens 99-108 19595796-6 2010 This is in contrast to myoglobin in water-glycerol, where the main solvent relaxation makes the strongest contribution to the calorimetric glass transition. Glycerol 42-50 myoglobin Homo sapiens 23-32 19442960-1 2009 This work presents an analysis of near environment of myoglobin (Mb) in different aqueous solutions (in the presence of NaCl, sucrose, trehalose, urea, and glycerol) using the coupled water fractions measured using a quartz crystal microbalance (QCM). Glycerol 156-164 myoglobin Homo sapiens 54-63 19442960-1 2009 This work presents an analysis of near environment of myoglobin (Mb) in different aqueous solutions (in the presence of NaCl, sucrose, trehalose, urea, and glycerol) using the coupled water fractions measured using a quartz crystal microbalance (QCM). Glycerol 156-164 myoglobin Homo sapiens 65-67 19442960-8 2009 The dynamics of coupled water in Mb with NaCl is the fastest (around 21 ps) and is slowest in glycerol (250 ps). Glycerol 94-102 myoglobin Homo sapiens 33-35 7892234-2 1995 The protein was protoporphyrin IX-substituted myoglobin in a glycerol/water solvent. Glycerol 61-69 myoglobin Homo sapiens 46-55 17388441-3 2007 Structural alteration of the protein was observed in native myoglobin glycerol solution and native myoglobin water solution. Glycerol 70-78 myoglobin Homo sapiens 60-69 17388441-9 2007 The hydrogen bond interaction and vibration-vibration interaction between the heme and solvent molecules dominates the energy transfer in native myoglobin aqueous solution and native myoglobin glycerol solutions. Glycerol 193-201 myoglobin Homo sapiens 145-154 17388441-9 2007 The hydrogen bond interaction and vibration-vibration interaction between the heme and solvent molecules dominates the energy transfer in native myoglobin aqueous solution and native myoglobin glycerol solutions. Glycerol 193-201 myoglobin Homo sapiens 183-192 17388441-10 2007 For modified myoglobin, the vibration-vibration interaction is also effective in glycerol solution, different from aqueous solution. Glycerol 81-89 myoglobin Homo sapiens 13-22 9463885-1 1998 We present the results of a comparative study of the binding of carbon monoxide to myoglobin in glycerol/buffer solution with different concentrations of guanidine hydrochloride, under extended illumination over the temperature range 30-80 K. The changes in the Soret band indicate that the folding state of the protein is a key parameter in determining the photodissociation process and the relaxation rate of the protein. Glycerol 96-104 myoglobin Homo sapiens 83-92 16506754-1 2006 Interconversion dynamics of the ligand in the primary docking site of myoglobin (Mb) and hemoglobin (Hb) in trehalose and glycerol/D2O mixtures at 283 K was investigated by probing time-resolved vibrational spectra of CO photolyzed from these proteins. Glycerol 122-130 myoglobin Homo sapiens 70-79 16506754-1 2006 Interconversion dynamics of the ligand in the primary docking site of myoglobin (Mb) and hemoglobin (Hb) in trehalose and glycerol/D2O mixtures at 283 K was investigated by probing time-resolved vibrational spectra of CO photolyzed from these proteins. Glycerol 122-130 myoglobin Homo sapiens 81-83 1615323-4 1992 The theory and experiment suggest that the dominant factor in markedly reducing the rate of conformational changes in myoglobin at low temperatures (less than 200 K) is the very high viscosity (greater than 10(7) centipoise) of the glycerol-water solvent. Glycerol 232-240 myoglobin Homo sapiens 118-127 8443162-0 1993 CO recombination to human myoglobin mutants in glycerol-water solutions. Glycerol 47-55 myoglobin Homo sapiens 26-35 8443162-1 1993 The kinetics of CO recombination to site-specific mutants of human myoglobin have been studied by flash photolysis in the temperature range 250-320 K on the nanosecond to second time scale in 75% glycerol at pH 7. Glycerol 196-204 myoglobin Homo sapiens 67-76 2990551-1 1985 Experiments were carried out to measure the effect of concentrations of glycerol on H-exchange (HX) rates by using myoglobin as a test protein. Glycerol 72-80 myoglobin Homo sapiens 115-124 2990551-4 1985 The effect of solvent glycerol on different parts of the HX curve of myoglobin was studied by use of a selective "kinetic labeling" approach. Glycerol 22-30 myoglobin Homo sapiens 69-78 907349-0 1977 The diffusion-controlled reaction kinetics of the binding of CO and O2 to myoglobin in glycerol-water mixtures of high viscosity. Glycerol 87-95 myoglobin Homo sapiens 74-83 7126544-1 1982 The kinetics of the reaction of CO with myoglobin have been studied by laser flash photolysis in glycerol-water as a function of solvent viscosity and temperature. Glycerol 97-105 myoglobin Homo sapiens 40-49 30021107-9 2018 We separately analyzed the effect of glycerol on the thermal stability of myoglobin at each hierarchical structural level. Glycerol 37-45 myoglobin Homo sapiens 74-83 32360459-0 2020 Insight into the binding of glycerol with myoglobin: Spectroscopic and MD simulation approach. Glycerol 28-36 myoglobin Homo sapiens 42-51 32360459-4 2020 In such studies, the researchers used spectroscopic and simulation approaches to study the alterations of the myoglobin structure and stability in glycerol presence. Glycerol 147-155 myoglobin Homo sapiens 110-119 32360459-5 2020 Experimental results showed a stability improvement of the complex myoglobin-glycerol. Glycerol 77-85 myoglobin Homo sapiens 67-76 32360459-9 2020 Molecular dynamics simulation showed that the glycerol presence could enhance myoglobin stability. Glycerol 46-54 myoglobin Homo sapiens 78-87 26656812-0 2015 Electroactive Film of Myoglobin Incorporated in a 3D-porous Calcium Alginate Film with Polyvinyl Alcohol, Glycerin and Gelatin. Glycerol 106-114 myoglobin Homo sapiens 22-31 26656812-1 2015 In this work, an electroactive porous Mb-CA"s composite film was fabricated by incorporating myoglobin (Mb) in a three-dimension (3D) porous calcium alginate (CA) film with polyvinyl alcohol, glycerol, and gelatin. Glycerol 192-200 myoglobin Homo sapiens 38-40 24291287-0 2014 Dielectric spectroscopy study of myoglobin in glycerol-water mixtures. Glycerol 46-54 myoglobin Homo sapiens 33-42 24291287-3 2014 Solutions of myoglobin in glycerol/water mixtures of various compositions are measured by dielectric spectroscopy in the frequency range from 10mHz to 10MHz. Glycerol 26-34 myoglobin Homo sapiens 13-22