Suppose there is a ligand binding pocket in this alpha-helix that contains residues of Leu (2), Phe (5), Gly (6), Ala (18), Tyr (22), Tyr (28), Gly (30), Cys (45), His (48) and Asp (49). What does this tell us about the likely nature or characteristics of a potential binding ligand? I said tha because 6/10 of the amino acids in this binding pocket are non-polar, that the ligand is also non-polar, but I think the question needs more description about the ligand. b) Briefly describe the driving forces and energetics behind folding of globular proteins (use terms like ΔH, ΔS, and ΔG) I said that H = -, S = +, G = - Folding driving force would likely be entropy change from non-polar residues interacting with a solvent (ex: water). Hence, non-polar residues would be buried in the globular protein structure from folding, causing entropy to increase for any liberated solvent molecules. Not 100% sure if this is correct, and explanation fails to account for H or G.
Structure and Composition of Cell Membrane
Despite differences in structure and function, all living cells in multicellular organisms are surrounded by a cell membrane. Just like the outer layer of the skin separates the body from its environment similarly, the cell membrane, also known as 'plasma membrane,' separates the inner content from its exterior environment.
Cell Membrane
The cell membrane is known by different names like plasma membrane or cytoplasmic membrane, or biological membrane. The term "cell membrane" was first introduced by C. Nageli and C. Cramer in the year 1855. Later on, in 1931, the term "plasmalemma" for cell membrane was given by J. Plowe. The cell membrane separates the cell's internal environment from the extracellular space. This separation allows the protection of cells from their environment.
Prokaryotes vs Eukaryotes
The cell is defined as the basic structural and functional unit of life. The cell membrane bounds it. It is capable of independent existence.
Consider a globular protein that contains an alpha-helix within it:
a) Suppose there is a ligand binding pocket in this alpha-helix that contains residues of Leu (2), Phe (5), Gly (6), Ala (18), Tyr (22), Tyr (28), Gly (30), Cys (45), His (48) and Asp (49). What does this tell us about the likely nature or characteristics of a potential binding ligand?
- I said tha because 6/10 of the amino acids in this binding pocket are non-polar, that the ligand is also non-polar, but I think the question needs more description about the ligand.
b) Briefly describe the driving forces and energetics behind folding of globular proteins (use terms like ΔH, ΔS, and ΔG)
- I said that H = -, S = +, G = -
- Folding driving force would likely be entropy change from non-polar residues interacting with a solvent (ex: water). Hence, non-polar residues would be buried in the globular protein structure from folding, causing entropy to increase for any liberated solvent molecules.
- Not 100% sure if this is correct, and explanation fails to account for H or G.
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