A5090818077- Protein Structure and Dynamics
- Enzyme Structure and Function
- Erythrocyte Function and Pathophysiology
- Amyloidosis: Diagnosis, Treatment, Outcomes
- Protein Hydrolysis and Bioactive Peptides
- Alzheimer's disease research and treatments
- Peptidase Inhibition and Analysis
- Enzyme Catalysis and Immobilization
- Neonatal Health and Biochemistry
- Monoclonal and Polyclonal Antibodies Research
- Meat and Animal Product Quality
- Plant Stress Responses and Tolerance
- RNA and protein synthesis mechanisms
- Metal and Thin Film Mechanics
- Lipid Membrane Structure and Behavior
- Insect Utilization and Effects
- Glycosylation and Glycoproteins Research
- Muscle metabolism and nutrition
- Pancreatic function and diabetes
- Neurobiology and Insect Physiology Research
- Phagocytosis and Immune Regulation
- Drug Transport and Resistance Mechanisms
- Microbial Metabolic Engineering and Bioproduction
- Ion Channels and Receptors
- Corrosion Behavior and Inhibition
Universidad Nacional Autónoma de México
2014-2024
Universidad Autónoma de la Ciudad de México
2015-2016
Medicina
2015-2016
Universidad Autónoma Metropolitana
1997-2007
Instituto de Diagnóstico e Investigaciones Metabólicas
1991
Light chain-associated amyloidosis is a fatal disease characterized by the aggregation and pathologic deposition of monoclonal light chain-related fragments as amyloid fibrils in organs or tissues throughout body. Notably, it has been observed that proteins encoded lambda variable chain (V(L)) gene segment 6a are invariably associated with deposition; however, contribution to this phenomenon not established. In regard, we have determined thermodynamic stability kinetics vitro fibrillogenesis...
Late embryogenesis abundant (LEA) proteins are part of a large protein family that protect other from aggregation due to desiccation or osmotic stresses. Recently, the Amarantus cruentus seed proteome was characterized by 2D-PAGE and one highly accumulated spot identified as Embryogenesis Abundant named AcLEA. In this work, AcLEA cDNA cloned into an expression vector recombinant purified characterized. encodes 172 amino acid polypeptide with predicted molecular mass 18.34 kDa estimated pI...
Abstract Transient protein–protein interactions are functionally relevant as a control mechanism in variety of biological processes. Analysis the 3D structure complexes indicates that water molecules trapped at interface very common; however, their role stability and specificity protein homodimer has been not addressed yet. To provide new insights into energetic bases govern formation highly hydrated interfaces, dissociation process bovine βlg variant A neutral pH was characterized here...
The ability to design stable proteins with custom-made functions is a major goal in biochemistry practical relevance for our environment and society. Understanding manipulating protein stability provide crucial information on the molecular determinants that modulate structure stability, expand applications of de novo proteins. Since (β/⍺)8-barrel or TIM-barrel fold one most common functional scaffolds, this work we designed collection TIM barrels (DeNovoTIMs), using computational...
Finding strategies to use the swim bladder of farmed totoaba (Totoaba macdonaldi) is utmost need reduce waste. Fish bladders are rich in collagen; hence, extracting collagen a promising alternative with benefits for aquaculture and environment. The elemental biochemical composition bladders, including their proximate amino acid compositions, was determined. Pepsin-soluble (PSC) used extract from its characteristics were analyzed. Alcalase papain preparation hydrolysates. Swim contained 95%...
Approximately 25% of the λ6 light chains have glycine rather than arginine at position 25, which is an allelic variant IGLV6‐57 ( 6a ) locus. The Gly25 has been shown to decrease folding stability germline V L protein 6aJL2 by 1.7 kcal·mol −1 . In this work, we compared thermodynamic and fibrillogenic properties amyloidosis (AL) derived recombinant (r) AR, contains Gly25, with those rV 6aJL2‐R25G disease‐associated proteins Wil Jto (myeloma). Our experiments show that four AR least stable;...
The reasons underlying the oligomeric nature of some proteins such as triosephosphate isomerase (TIM) are unclear. It has been proposed that this enzyme is an oligomer, mainly because its stability rather than for functional reasons. To address issue, reversible denaturation and renaturation homodimeric TIM from baker's yeast (Saccharomyces cerevisiae) induced by guanidinium chloride urea have characterized spectroscopic, hydrodynamic techniques. unfolding refolding not coincident after...
The reversible thermal unfolding of oligomeric TIM barrels results from a delicate balance physicochemical properties related to the sequence, native and unfolded states transition between them.
The effect of urea and guanidine hydrochloride (GdmCl) on the activity heart lactate dehydrogenase, glycerol-3-phosphate hexokinase, inorganic pyrophosphatase, glyceraldehyde-3-phosphate dehydrogenase was studied in low-water systems. Most experiments were made a system formed with toluene, phospholipids, Triton X-100, water range that varied over 1.0-6.5% (by vol.) [Garza-Ramos, G., Darszon, A., Tuena de Gómez-Puyou, M. & A. (1990) Biochemistry 29, 751-757]. In such conditions at saturating...
Abstract Variable domain (V L ) gene segments exhibit variable tendencies to be associated with light chain amyloidosis (AL). While few of them are very frequent in AL and give rise most the amyloidogenic chains compiled at sequence databases, other rarely found among cases. To analyze which extent these depend on folding stability aggregation propensity germline V protein, we characterized proteins encoded by four AL-associated one not AL. We that rV differ widely conformational vitro...
The study of binding thermodynamics is essential to understand how affinity and selectivity are acquired in molecular complexes. Periplasmic proteins (PBPs) macromolecules biotechnological interest that bind a broad number ligands have been used design biosensors. lysine-arginine-ornithine protein (LAO) PBP 238 residues binds the basic amino acids l-arginine l-histidine with nm μm affinity, respectively. It has shown difference for arginine histidine caused by enthalpy, this correlates...
We have isolated a cDNA clone of the glycolytic enzyme, triosephosphate isomerase (TPI) from Entamoeba histolytica. Degenerate oligonucleotides obtained by reverse translation conserved poly‐peptide sequences, derived TPIs other organisms, were used to amplify 450‐bp fragment using E. histolytica as template. The was screen library. cDNA, encoding protein 261 amino acids, shares 43–52.6% positional identity with known protozoan TPIs. catalytic residues conserved; nevertheless, several indels...
In mesophiles, triosephosphate isomerase (TIM) is an obligated homodimer. We have previously shown that monomeric folding intermediates are common in the chemical unfolding of TIM, where dissociation provides 75% overall conformational stability dimer. However, analysis crystallographic structure shows that, during unfolding, intermonomeric contacts contribute to only 5% increase accessible surface area. this work several methodologies were used characterize thermal and TIM from Entamoeba...
Triosephosphate isomerase from Saccharomyces cerevisiae (wt-TIM) is an obligated homodimer. The interface of wt-TIM formed by 34 residues. In the native dimer, each monomer buries nearly 2600 Å2 accessible surface area (ASA), and 58.4% ASA hydrophobic. We determined thermodynamic functional consequences increasing hydrophobic character interface. Mutations were restricted to a cluster five nonconserved residues located far active site. Two different approaches, in silico design directed...
Reactive oxidative species (ROS) and S-glutathionylation modulate the activity of plant cytosolic triosephosphate isomerases (cTPI). Arabidopsis thaliana cTPI (AtcTPI) is subject redox regulation at two reactive cysteines that function as thiol switches. Here we investigate role these residues, AtcTPI-Cys13 At-Cys218, by substituting them with aspartic acid mimics irreversible oxidation cysteine to sulfinic amino acids mimic conjugation. Crystallographic studies show mimicking promotes...
Triosephosphate isomerase (TIM) is a dimeric enzyme formed by two identical (β/α)8 barrels. In this work, we compare the unfolding and refolding of TIMs from Entamoeba histolytica (EhTIM) baker's yeast (yTIM). A monomeric intermediate was detected in GdnHCl-induced EhTIM. The thermodynamic, spectroscopic, catalytic, hydrodynamic properties were found to be very similar those previously described for yTIM observed GdnHCl. Monomer reversible both TIMs; however, dissociation step irreversible...