Alright my friend basically it would be 30% our atmosphere and clouds are the one who do it if were more than 30% there would be a lot higher risk of cancer
In a parallel circuit, the voltage across each of the components is the same, and the total current is the sum of the currents
through each component.
If two or more components are connected in parallel they have the same potential difference (
voltage)
across their ends. The potential differences across
the components are the same in magnitude, and they also have identical
polarities. The same voltage is applicable to all circuit
components connected in parallel.
If each bulb is wired to the battery in a separate loop, the bulbs are said to be in parallel.
A constant stream of charged particles flowing away form the sun
Answer:
It helps us to see things.
It helps plants to make food and grow.
It is used in power satellites and space stations.
It is used in many electronic appliances.
The energy of light from the sun can be harvested to solar panels and can be used for domestic use since it is eco-friendly and cost effective too.
Explanation:
Answer:
a) The response indicates that a pH below or above this range will most likely cause enolase to denature/change its shape and be less efficient or unable to catalyze the reaction.
b)The response indicates that the appropriate negative control is to measure the reaction rate (at the varying substrate concentrations) without any enzyme present.
c)The response indicated that the enolase has a more stable/functional/correct/normal protein structure at the higher temperature of 55°C than at 37°C because the enzyme is from an organism that is adapted to growth at 55°C.
Explanation:
Enolase catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate during both glycolysis and gluconeogenesis.In bacteria, enolases are highly conserved enzymes and commonly exist as homodimers.
The temperature optimum for enolase catalysis was 80°C, close to the measured thermal stability of the protein which was determined to be 75°C, while the pH optimum for enzyme activity was 6.5. The specific activities of purified enolase determined at 25 and 80°C were 147 and 300 U mg−1 of protein, respectively. Km values for the 2-phosphoglycerate/phosphoenolpyruvate reaction determined at 25 and 80°C were 0.16 and 0.03 mM, respectively. The Km values for Mg2+ binding at these temperatures were 2.5 and 1.9 mM, respectively.
Enolase-1 from Chloroflexus aurantiacus (EnoCa), a thermophilic green non-sulfur bacterium that grows photosynthetically under anaerobic conditions. The biochemical and structural properties of enolase from C. aurantiacus are consistent with this being thermally adapted.
