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- Universidade Federal de Goiás; BR; UFG; Mestrado em Nutricao e Saude; Ciencias da Saude
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- La Sapienza Universidade de Roma
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Effects of a Low-Protein Diet on Plasma Amino Acid and Homocysteine Levels and Oxidative Status in Rats
Effects of dietary urea levels on milk protein fractions of Holstein cows
Suplementação protéica, uso de subprodutos agroindustriais e processamento de milho em dietas para vacas leiteiras em confinamento.; Protein supplementation, by-products and corn processing for lactating dairy cows.
Efeito Hipocolesterolemizante da Proteína de Amaranto (Amaranthus cruentus BRS-Alegria) em Hamsters ; Cholesterol-lowering effect of amaranth protein (Amaranthus cruentus L. BRS-Alegria) in hamsters.
Efeito do feijão caupi (Vigna unguiculata L. Walp) e da proteína isolada no metabolismo lipídico em hamsters hipercolesterolemizados; Effect of the whole seed and protein isolate of cowpea (Vigna unguiculata L. Walp) on the lipid metabolism of hypercholesterolemic hamsters
A proteína ligadora dos ácidos graxos Sm14 de Schistosoma mansoni: estrutura gênica, polimorfismo, expressão heteróloga em E. coli e significado estrutural e funcional das suas formas polimórficas e mutantes; The Sm14 Schistosoma mansoni fatty acid binding protein: gene structure, polymorphism, heterologus expression in E. coli and structure-functional study of her polymorphic and mutant forms
Suplementação com aminoácios de cadeia ramificada atenua em proles os efeitos mediados pela dieta materna restrita em proteína; Branched-chain amino acids supplementation attenuates in offspring the effects mediated by maternal protein-restrict diet.
Serum and Urinary C-Reactive Protein Concentrations in Dogs with Leptospirosis
Evaluation of a protein deficient diet in rats through blood oxidative stress biomarkers
Experimental mixture design as a tool for proteases production by Aspergillus niger and obtaining of protein hydrolysates with multiple functional and biological properties; Aplicação da ferramenta de planejamento experimental de misturas como estratégia para a produção de proteases por Aspergillus niger e obtenção de hidrolisados proteicos com múltiplas propriedades funcionais e biológicas
Statistics and Physical Origins of pK and Ionization State Changes upon Protein-Ligand Binding
Eficácia alimentar e qualidade proteica de misturas de caseína com gelatina em dietas com baixos teores de proteína; Food and protein efficiency mixtures of gelatin with casein in diets with low levels of protein
The effect of higher protein human milk fortifier on growth in preterm infants.
Parallel and miniaturised Analysis of Protein-Protein Interactions in T-Cell Signal Transduction by Fluorescence Cross-Correlation Spectroscopy and Peptide Microarrays; Parallele und miniaturisierte Analyse von Protein-Protein-Interaktionen in der T-Zell-Signaltransduktion mittels Fluoreszenz-Kreuzkorrelations-Spektroskopie und Peptidmikroarrays
Modeling Flexibility of Protein-DNA and Protein-Ligand Complexes using Molecular Dynamics; Modellierung der Flexibilität von Protein-DNA und Protein-Ligand Komplexen mit Hilfe von Molekulardynamischen Simulationen
Resource for benchmarking the applicability of protein structure models
Pattern Discovery in Protein Structures and Interaction Networks
Development and Application of a quantitative Mass spectrometry based Platform for Thermodynamic Analysis of Protein interaction Networks
The identification and quantification of protein-protein interactions in large scale is critical to understanding biological processes at a systems level. Current approaches for the analysis of protein -protein interactions are generally not quantitative and largely limited to certain types of interactions such as binary and strong binding interactions. They also have high false-positive and false-negative rates. Described here is the development of and application of mass spectrometry-based proteomics metehods to detect and quantify the strength of protein-protein and protein-ligand interactions in the context of their interaction networks. Characterization of protein-protein and protein-ligand interactions can directly benefit diseased state analyses and drug discovery efforts.
The methodologies and protocols developed and applied in this work are all related to the Stability of Unpurified Proteins from Rates of amide H/D Exchange (SUPREX) and Stability of Protein from Rates of Oxidation (SPROX) techniques, which have been previously established for the thermodynamic analysis of protein folding reactions and protein-ligand binding interactions. The work in this thesis is comprised of four parts. Part I involves the development of a Histidine Slow H/D exchange protocol to facility SURPEX-like measurements on the proteomic scale. The Histidine Slow H/D exchange protocol is developed in the context of selected model protein systems and used to investigate the thermodynamic properties of proteins in a yeast cell lysate.
In Part II an isobaric mass tagging strategy is used in combination with SPROX (i.e....
Kinetic Characterization of the Coupled Folding and Binding Mechanism of Bacterial RNase P Protein: an Intrinsically Unstructured Protein
Understanding the interconversion between the thermodynamically distinguishable states present in a protein folding pathway provides not only the kinetics and energetics of protein folding but also insights into the functional roles of these states in biological systems. The protein component of bacterial RNase P holoenzyme from Bacillus subtilis (P protein) was used as a model system to elucidate the general folding/unfolding of an intrinsically unstructured protein (IUP) both in the absence and presence of ligands.
P protein was previously characterized as an intrinsically unstructured protein, and it is predominantly unfolded in the absence of ligands. Addition of small anions can induce the protein to fold. Therefore, the folding and binding are tightly coupled. Trimethylamine-N oxide (TMAO), an osmolyte that stabilizes the unliganded folded form of the protein, enabled us to study the folding process of P protein in the absence of ligand. Transient stopped-flow kinetic time courses at various final TMAO concentrations showed multiphase kinetics. Equilibrium "cotitration" experiments were performed using both TMAO and urea to obtain a TMAO-urea titration surface of P protein. Both kinetic and equilibrium studies show evidence of an intermediate state in the P protein folding process. The intermediate state is significantly populated and the folding rate constants involved in the reaction are slow relative to similar size proteins.
NMR spectroscopy was used to characterize the structural properties of the folding intermediate of P protein. The results indicate that the N-terminal (residues 2-19) and C-terminal regions (residues 91-116...