The client is most likely in the exhaustion stage of the general adaptation syndrome.
Because they have so many children at once.
Answer: 0.05 M
Explanation:
Para responder esta pregunta, hay que tener en cuenta la Ley de Conservación de la Masa. <u>La misma indica que en una reacción química en un sistema cerrado, la masa total de las moléculas que participan permanece constante.</u> Esto significa que la masa utilizada en los reactivos es la misma que la masa de los productos generados.
En este problema, se cuenta con una solución de NaOH (hidróxido de sodio) tiene una molaridad de 0.204 (siendo la molaridad el número de moles por litro de solución) y se utilizan 16.4 mL de dicha solución para agregarla a 50 mL de una solución de H3PO4 (ácido fosfórico).
Entonces, ya que la masa de ambas soluciones no se pierde, podemos utilizar la ecuación de la Ley de Conservación de la Masa:
Concentración inicial x Volumen inicial = Concentración final x Volumen final.
Concentración inicial: 0.204 M
Volumen inicial: 16.4 mL
Concentración final: ?
Volumen final: 50 mL + 16.4 mL = 66.4 mL
Reemplazamos los valores en la ecuación:
0.204 M x 16.4 mL = Concentración final x 66.4 mL
La molaridad de la solución de H3PO4 es de 0.05 M.
4) A dietician helps the patient get the amount of nutrients they need, they can also assist in healthy weight loss for a patient who’s prepping for surgical procedure
Answer:
One of the common genetic disorders is sickle cell anemia, in which 2 recessive alleles must meet to allow for destruction and alteration in the morphology of red blood cells. This usually leads to loss of proper binding of oxygen to hemoglobin and curved, sickle-shaped erythrocytes. The mutation causing this disease occurs in the 6th codon of the HBB gene encoding the hemoglobin subunit β (β-globin), a protein, serving as an integral part of the adult hemoglobin A (HbA), which is a heterotetramer of 2 α chains and 2 β chains that is responsible for binding to the oxygen in the blood. This mutation changes a charged glutamic acid to a hydrophobic valine residue and disrupts the tertiary structure and stability of the hemoglobin molecule. Since in the field of protein intrinsic disorder, charged and polar residues are typically considered as disorder promoting, in opposite to the order-promoting non-polar hydrophobic residues, in this study we attempted to answer a question if intrinsic disorder might have a role in the pathogenesis of sickle cell anemia. To this end, several disorder predictors were utilized to evaluate the presence of intrinsically disordered regions in all subunits of human hemoglobin: α, β, δ, ε, ζ, γ1, and γ2. Then, structural analysis was completed by using the SWISS-MODEL Repository to visualize the outputs of the disorder predictors. Finally, Uniprot STRING and D2P2 were used to determine biochemical interactome and protein partners for each hemoglobin subunit along with analyzing their posttranslational modifications. All these properties were used to determine any differences between the 6 different types of subunits of hemoglobin and to correlate the mutation leading to sickle cell anemia with intrinsic disorder propensity.
Explanation:
