Answer:
as a dimer consisting of two identical monomers (80 kDa subunits) that are packed together via hydrophobic interactions
Explanation:
SDS-PAGE (sodium dodecyl sulphate–polyacrylamide gel electrophoresis), is an electrophoretic methodology used to separate proteins that have a molecular weight between 5 to 250 kDa. SDS is a well-known ionic detergent that is able to break hydrophobic interactions and hydrogen bonds. Moreover, size-exclusion chromatography is a filtration technique that separates molecules in solution according to their molecular size. In this case, SDS-PAGE showed that the target protein is composed of two identical subunits (monomers) of 80 kDa each, which were separated by the detergent and formed one single band in the SDS-PAGE gel.
Auroras normally occur in the Earth's thermosphere.
Answer:
<u><em>This is because the enzymes might work best at higher temperature than 37 degrees Celsius. Increase in temperature will increase the catalysis of the reaction.</em></u>
Explanation:
<em>When the temperature is increased, the molecules possess greater kinetic energy. This will allow more substrate and enzymes to collide. As a result, there will be more enzymes taking place in the reaction which will cause the rate of the reaction to increase.</em>
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However, if the temperature goes too high, then the shape of the active site of the enzymes will get changed. The enzyme will deactivate and the reaction will stop.
1. The binding of an inhibitor can stop a substrate from entering the enzyme's active site and/or hinder the enzyme from catalyzing its reaction. Inhibitor binding is either reversible or irreversible. Irreversible inhibitors usually react with the enzyme and change it chemically (e.g. via covalent bond formation).
2. Carbon has four valence electrons, so it can achieve a full outer energy level by forming four covalent bonds.
hope this helps
Pressure would be my best guess, since no choices were given.
