Search results for " myoglobin"
showing 9 items of 9 documents
Biopreservation of Myoglobin in Crowded Environment: A Comparison between Gelatin and Trehalose Matrixes.
2017
Biopreservation by sugar and/or polymeric matrixes is a thoroughly studied research topic with wide technological relevance. Ternary amorphous systems containing both saccharides and proteins are extensively exploited to model the in vivo biopreservation process. With the aim of disentangling the effect of saccharides and polypeptidic crowders (such as gelatin) on the preservation of a model protein, we present here a combined differential scanning calorimetry and UV-vis spectrophotometry study on samples of myoglobin embedded in amorphous gelatin and trehalose + gelatin matrixes at different hydrations, and compare them with amorphous myoglobin-only and myoglobin-Trehalose samples. The res…
Cyanide binding and heme cavity conformational transitions in **Drosophila melanogaster** hexacoordinate hemoglobin
2006
The reason for the presence of hemoglobin-like molecules in insects, such as Drosophila melanogaster, that live in fully aerobic environments has yet to be determined. Heme endogenous hexacoordination (where HisE7 and HisF8 axial ligands to the heme Fe atom are both provided by the protein) is a recently discovered mechanism proposed to modulate O-2 affinity in hemoglobins from different species. Previous results have shown that D. melanogaster hemoglobin 1 (product of the glob1 gene) displays heme endogenous hexacoordination in both the ferrous and ferric states. Here we present kinetic data characterizing the exogenous cyanide ligand binding process, and the three-dimensional structure (a…
Tracking the structural dynamics of proteins in solution using time-resolved wide-angle X-ray scattering
2008
We demonstrate tracking of protein structural changes with time-resolved wide-angle X-ray scattering (TR-WAXS) with nanosecond time resolution. We investigated the tertiary and quaternary conformational changes of human hemoglobin under nearly physiological conditions triggered by laser-induced ligand photolysis. We also report data on optically induced tertiary relaxations of myoglobin and refolding of cytochrome c to illustrate the wide applicability of the technique. By providing insights into the structural dynamics of proteins functioning in their natural environment, TR-WAXS complements and extends results obtained with time-resolved optical spectroscopy and X-ray crystallography.
Molecular dynamics simulation of sucrose- and trehalose-coated carboxy-myoglobin
2005
We performed a room temperature molecular dynamics (MD) simulation on a system containing 1 carboxy-myoglobin (MbCO) molecule in a sucrose–water matrix of identical composition (89% [sucrose/(sucrose + water)] w/w) as for a previous trehalose–water–MbCO simulation (Cottone et al., Biophys J 2001;80:931–938). Results show that, as for trehalose, the amplitude of protein atomic mean-square fluctuations, on the nanosecond timescale, is reduced with respect to aqueous solutions also in sucrose. A detailed comparison as a function of residue number evidences mobility differences along the protein backbone, which can be related to a different efficacy in bioprotection. Different heme pocket struc…
Proteins in Saccharides Matrices and the Trehalose Peculiarity: Biochemical and Biophysical Properties
2015
Immobilization of proteins and other biomolecules in saccharide matrices leads to a series of peculiar properties that are relevant from the point of view of both biochemistry and biophysics, and have important implications on related fields such as food industry, pharmaceutics, and medicine. In the last years, the properties of biomolecules embedded into glassy matrices and/or highly concentrated solutions of saccharides have been thoroughly investigated, at the molecular level, through in vivo, in vitro, and in silico studies. These systems show an outstanding ability to protect biostructures against stress conditions; various mechanisms appear to be at the basis of such bioprotection, th…
Elastic neutron scattering of dry and rehydrated trehalose coated carboxy-myoglobin
2008
We report here a comparison between the hydrogen atoms mean square displacements measured by elastic neutron scattering on trehalose coated carboxy-myoglobin, at ILL on the backscattering spectrometers IN13 and IN16. An inconsistency is observed when comparing the mean square displacements measured on the two spectrometer, on samples of identical composition, since they resulted of larger amplitude on IN13 (either in condition of drought or after overnight rehydration under 75% D2O atmosphere), notwithstanding the lower time window accessible on this instrument with respect to IN16. Such inconsistency disappears when the data obtained on this last spectrometer are analyzed in two separate r…
Calorimetric study of myoglobin embedded in trehalose-water matrixes
2009
It has been suggested that in ‘dry’ protein–trehalose–water systems, water–mediated hydrogen bond network, whose strength increases by drying, anchors the protein to its surroundings. To further characterize this effect, we performed a DSC study on low-water myoglobin–trehalose systems. The denaturation temperature resulted to increase by decreasing hydration, and linearly correlated to the glass transition temperature of both the ternary protein–water–trehalose and the binary water–trehalose systems. Further measurements are being performed to investigate eventual differences among different saccharides.
The effects of rapid weight loss on skeletal muscle in judo athletes
2020
Abstract Objective To observe the effect of rapid weight loss (RWL) methods over 3 days on muscle damage in judokas. Methods Eighteen judokas participated in this crossover study, meaning that judo athletes were subjected to exercise-only phase (4 days) and RWL phase (3 days). Subjects were tested for myoglobin, creatine kinase, aldolase, hemoglobin, and hematocrit values on seven consecutive days. These biomarkers served as indicators of acute muscle damage. Results During the exercise-only phase, no significant changes were observed. Myoglobin (Mb) (p < 0.001), creatine kinase (CK) (p < 0.001) and aldolase (ALD) (p < 0.001) significantly increased only during the RWL phase, as we…