why the transmembrane regions of many membrane bound proteins are α- helices?
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A transmembrane protein (TP) is a type of integral membrane protein that spans the entirety of the cell membrane to which it is permanently attached. Many transmembrane proteins function as gateways to permit the transport of specific substances across the membrane. They frequently undergo significant conformational changes to move a substance through the membrane.
Transmembrane proteins are polytopic proteins that aggregate and precipitate in water. They require detergents or nonpolar solvents for extraction, although some of them (beta-barrels) can be also extracted using denaturing agents.
The peptide sequence that spans the membrane is largely hydrophobic, allowing for transmembrane prediction methods such as the hydropathy plot. Despite this, there are variations in polarity along the length of the transmembrane sequence. The polarity depends greatly on whether the location under investigation is facing the surrounding lipid molecules or facing an aqueous pore.[1]
The other type of integral membrane protein is the integral monotopic protein that is also permanently attached to the cell membrane but does not pass through it.[2]
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Transmembrane proteins are polytopic proteins that aggregate and precipitate in water. They require detergents or nonpolar solvents for extraction, although some of them (beta-barrels) can be also extracted using denaturing agents.
The peptide sequence that spans the membrane is largely hydrophobic, allowing for transmembrane prediction methods such as the hydropathy plot. Despite this, there are variations in polarity along the length of the transmembrane sequence. The polarity depends greatly on whether the location under investigation is facing the surrounding lipid molecules or facing an aqueous pore.[1]
The other type of integral membrane protein is the integral monotopic protein that is also permanently attached to the cell membrane but does not pass through it.[2]
(plz mark my answer as brainlist my friend)
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