Search results for "MYOGLOBIN"
showing 10 items of 141 documents
Role of Solvent on Protein-Matrix Coupling in MbCO Embedded in Water-Saccharide Systems: A Fourier Transform Infrared Spectroscopy Study
2006
AbstractEmbedding protein in sugar systems of low water content enables one to investigate the protein dynamic-structure function in matrixes whose rigidity is modulated by varying the content of residual water. Accordingly, studying the dynamics and structure thermal evolution of a protein in sugar systems of different hydration constitutes a tool for disentangling solvent rigidity from temperature effects. Furthermore, studies performed using different sugars may give information on how the detailed composition of the surrounding solvent affects the internal protein dynamics and structural evolution. In this work, we compare Fourier transform infrared spectroscopy measurements (300–20K) o…
Hydration dependent dynamics in sol-gel encapsulated myoglobin.
2008
In this work we study the effect of hydration on the dynamics of a protein in confined geometry, i.e. encapsulated in a porous silica matrix. Using elastic neutron scattering we investigate the temperature dependence of the mean square displacements of non-exchangeable hydrogen atoms of sol-gel encapsulated met-myoglobin. The study is extended to samples at 0.2, 0.3 and 0.5 g water/g protein fractions and comparison is made with met-myoglobin powders at the same average hydration and with a dry powder sample. Elastic data are analysed using a model of dynamical heterogeneity to take into account deviations of elastic intensity from gaussian behaviour in a large momentum transfer range and r…
Thermal evolution of the CO stretching band in carboxy-myoglobin in the light of neutron scattering and molecular dynamics simulations
2008
Abstract As it is well known, the thermal behaviour of the CO stretching band in MbCO reflects the interconversion among protein’s taxonomic and lower tier substates. We compare here FTIR data on the thermal behaviour of the CO stretching band in MbCO embedded in non-liquid, water–trehalose matrixes, and neutron scattering data on dry and hydrated proteins and nucleic acids. The comparison, also in the light of simulative data, gives relevant information on the relationship between the mean square displacements of hydrogen atoms and the heme pocket thermal rearrangements in MbCO, as experienced by the bound CO, in the temperature region 100–200 K, and at higher temperature when large scale …
Spectroscopic markers of the T-R quaternary transition in human hemoglobin
2004
n questo lavoro, usiamo un protocollo sol-gel per intrappolare e confrontare gli stati quaternari R e T di entrambi i deossigenati (deossiHb) ederivati di ossido di carbonio (HbCO) dell'emoglobina umana. La banda di assorbimento ottico del vicino infrarosso III e lo stretching di CO a infrarossibanda sono utilizzati per rilevare l'effetto della struttura quaternaria sulle proprietà spettrali di deoxyHb e HbCO; confronto con mioglobinaconsente una valutazione dei contributi terziari e quaternari ai turni di banda misurati. La RXLa transizione T è indicata per causare un bluspostamento della banda III di ~ 35 cm?1per deoxyHb e uno spostamento rosso della banda di allungamento CO di soli ~ 0…
Myoglobin on Silica: A Case Study of the Impact of Adsorption on Protein Structure and Dynamics
2013
International audience; If protein structure and function changes upon adsorption are well documented, modification of adsorbed protein dynamics remains a blind spot, despite its importance in biological processes. The adsorption of metmyoglobin on a silica surface was studied by isotherm measurements, microcalorimetry, circular dichroïsm, and UV-visible spectroscopy to determine the thermodynamic parameters of protein adsorption and consequent structure modifications. The mean square displacement and the vibrational densities of states of the adsorbed protein were measured by elastic and inelastic neutron scattering experiments. A decrease of protein flexibility and depletion in low freque…
Light-Induced Protein-Matrix Uncoupling and Protein Relaxation in Dry Samples of Trehalose-Coated MbCO at Room Temperature
2005
In humid samples of trehalose-coated carboxy-myoglobin (MbCO), thermally driven conformational relaxation takes place after photodissociation of the carbon monoxide (CO) molecule at room temperature. In such samples, because of the extreme viscosity of the external matrix, photodissociated CO cannot diffuse out of the protein and explores the whole (proximal and distal side) heme pocket, experiencing averaged protein heme pocket structures, as a result of the presence of Brownian motions. At variance, in very dry samples, a lower portion of the photodissociated CO diffuses from the distal to the proximal heme pocket side probing in nonaveraged structures. We revisit here the flash photolysi…
Multimarker risk strategy for predicting 1-month and 1-year major events in non-ST-elevation acute coronary syndromes.
2005
The aim of this study was to define the utility of the combined measurement of troponin I, myoglobin, C-reactive protein, fibrinogen, and homocysteine to predict risk in non-ST elevation acute coronary syndromes.Troponin I, myoglobin, high-sensitivity C-reactive protein, fibrinogen, and homocysteine were measured in 557 consecutive patients admitted to our institution for non-ST elevation acute coronary syndrome. The risk for major events (death or nonfatal myocardial infarction) at first month and at first year follow-up was analyzed.In a multivariate model adjusting for baseline characteristics and electrocardiographic changes, the only biomarkers related to major events at first month we…
Structural factors controlling ligand binding to myoglobin: a kinetic hole-burning study.
1998
Using temperature-derivative spectroscopy in the temperature range below 100 K, we have studied the dependence of the Soret band on the recombination barrier in sperm whale carbonmonoxy myoglobin (MbCO) after photodissociation at 12 K. The spectra were separated into contributions from the photodissociated species, Mb*CO, and CO-bound myoglobin. The line shapes of the Soret bands of both photolyzed and liganded myoglobin were analyzed with a model that takes into account the homogeneous bandwidth, coupling of the electronic transition to vibrational modes, and static conformational heterogeneity. The analysis yields correlations between the activation enthalpy for rebinding and the model p…
Comparison of neutron and X-ray scattering of dilute myoglobin solutions.
1975
Experimental results obtained by neutron scattering of dilute solutions of myoglobin are compared with those obtained by X-ray scattering. X-ray scattering remains the more powerful technique at wider angles above 0.3 A−1, where neutron experiments are less accurate because of low coherent scattering probability and high incoherent background. Neutron scattering is preferable at momentum transfers below 0.2 A−1; the conditions for applying the contrast variation method for the evaluation of the three basic scattering functions, which are due to shape and internal structure, equation (3), are ideally fulfilled in this region. Furthermore, neutrons allow observation of the hydrogen-deuterium …
Androglobin: a chimeric globin in metazoans that is preferentially expressed in mammalian testes
2012
Abstract: Comparative genomic studies have led to the recent identification of several novel globin types in the Metazoa. They have revealed a surprising evolutionary diversity of functions beyond the familiar O2 supply roles of hemoglobin and myoglobin. Here we report the discovery of a hitherto unrecognized family of proteins with a unique modular architecture, possessing an N-terminal calpain-like domain, an internal, circular permuted globin domain, and an IQ calmodulin-binding motif. Putative orthologs are present in the genomes of many metazoan taxa, including vertebrates. The calpain-like region is homologous to the catalytic domain II of the large subunit of human calpain-7. The glo…