Hydrophobic amino acids are buried at the core of a water-soluble globular protein.
<h3>What makes globular proteins water soluble?</h3>
Numerous hundreds to thousands of amino acids are used to make proteins. The arrangement of amino acids within a protein molecule determines its ultimate form. A protein molecule is classified into two classes—fibrous proteins and globular proteins—based on its final shape.
The structure of globular proteins resembles a ball or a globe. A globular structure is created by the folding of different amino acid chains. The two most significant globular proteins present in the human body are hemoglobin and myoglobin. The hydrophobic side chains of the amino acids are hidden inside the cores of the domains whereas the hydrophilic side chains are located on the surface of the molecule thanks to the arrangement of the amino acids.
The hydrophobic amino acids can be buried in the center of globular proteins due to interactions between the hydrophobic groups in their side chains. This is the fundamental property of globular proteins that makes them water soluble.
Examples of hydrophobic amino acids are phenylalanine, alanine, valine, etc.
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Sweat glands sorry if im wrong not sure
For each glucose that enters glycolysis, 10 NADH enter the electron transport chain.
- NADH and FADH, which function as electron transporters as they move through the inner membrane region, are involved in the processes of the electron transport chain.
- Electrons are transferred from NADH to the electron transport chain at complex I, where they transit through the other complexes. In this mechanism, NADH is oxidized to NAD.
- The four protein complexes of the electron transport chain use this energy to oxidize NADH and FADH2 (ETC).
- Each of the three previous stages of respiration—glycolysis, the conversion of pyruvate into acetyl-CoA, and the citric acid cycle—contributes two of the ten NADH molecules that enter the electron transport.
- The citric acid cycle contributes six of the molecules. The citric acid cycle is where the two FADH2 come from.
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