Answer:
glucose is in large sugar molecules, while fructose is in simple fruits and vegetables
The 7160 cal energy is required to melt 10. 0 g of ice at 0. 0°C, warm it to 100. 0°C and completely vaporize the sample.
Calculation,
Given data,
Mass of the ice = 10 g
Temperature of ice = 0. 0°C
- The ice at 0. 0°C is to be converted into water at 0. 0°C
Heat required at this stage = mas of the ice ×latent heat of fusion of ice
Heat required at this stage = 10 g×80 = 800 cal
- The temperature of the water is to be increased from 0. 0°C to 100. 0°C
Heat required for this = mass of the ice×rise in temperature×specific heat of water
Heat required for this = 10 g×100× 1 = 1000 cal
- This water at 100. 0°C is to be converted into vapor.
Heat required for this = Mass of water× latent heat
Heat required for this = 10g ×536 =5360 cal
Total energy or heat required = sum of all heat = 800 +1000+ 5360 = 7160 cal
to learn more about energy
brainly.com/question/7185299
#SPJ4
i speak english . gracias!
Answer:
-12.3 degrees F.
Originally Answered: At what temperature does the Kelvin scale read double the Fahrenheit reading? -24.6 degrees C = -12.3 degrees F.
Explanation:
<h3><u>Answer;</u></h3>
The statements that are True are;
- Upon binding a molecule of oxygen, Hb undergoes a conformational change that makes the binding of subsequent O2 molecules easier.
- The conformational change induced in Hb upon binding oxygen is the result of a small movement (0.2 Å) of the iron cation in the center of heme.
- Site-directed mutagenesis studies have indicated that the cooperativity of O2 binding in Hb is attributable to the movement of the F helix in Hb.
<h3><u>Explanation</u>;</h3>
- Hemoglobin is a key pigment in the blood that transports oxygen gas to all the tissues in the body. It is made up of two types of chains; that is two alpha chains and two beta chains.
- in its deoxygenated state hemoglobin has a low affinity for oxygen compared to myoglobin. When oxygen is bound to the first subunit of hemoglobin it leads to subtle changes to the quaternary structure of the protein. This in turn makes it easier for a subsequent molecule of oxygen to bind to the next subunit.