Answer:
I would say the last one because mass is not created nor destroyed.
Explanation:
Answer:
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- <u><em>Because the x-intercet of the graph represents volume zero, which indicates the minimum possible temperature or absolute zero.</em></u>
Explanation:
Charle's Law for ideal gases states that, at constant pressure, the <em>temperature</em> and the <em>volume</em> of a sample of gas are protortional.

That means that the graph of the relationship between Temperature, in Kelivn, and Volume is a line, which passes through the origin.
When you work with Temperature in Celsius, and the temperature is placed on the x-axis, the line is shifted to the left 273.15ºC.
Meaning that the Volume at 273.15ºC is zero.
You cannot reach such low temperatures in an experiment, and also, volume zero is not real.
Nevertheless, you can draw the line of best fit and extend it until the x-axis (corresponding to a theoretical volume equal to zero), and read the corresponding temperature.
Subject to the experimental errors, and the fact that the real gases are not ideal, the temperature that you read on the x-axis is the minimum possible temperature (<em>absolute zero</em>) as the minimum possible volume is zero.
<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.
Answer:
What is the kinetic energy of a 2kg rabbit hopping at a speed of 1.25 m/s?1,5625J