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What type of amino acid side chain would you expect to find on the surface of a protein embedded in a cell membrane?
You would expect to find hydrophobic amino acid side chains on the surface of a protein embedded in a cell membrane. These hydrophobic side chains interact favorably with the hydrophobic lipid bilayer of the membrane, helping the protein to stay anchored in the membrane.
What amino acids would be most likely found buried deep within the interior of a protein?
Hydrophobic amino acids such as leucine, isoleucine, valine, and phenylalanine are typically found buried deep within the interior of a protein due to their non-polar nature. This helps to maintain the structural integrity of the protein by minimizing interactions with water molecules.
The r group or side chain of the amino acid serine is -ch2-oh the r group or side chain of the amino acid alanine is -ch3 where would you expect to find these amino acids in a globular protein in aq?
Serine, being hydrophilic, will be more likely to appear near the surface of a globular protein in solution, and alanine, being hydrophobic, will more likely appear near the centre of the protein. This illustrates the "hydrophobic effect", which is one of the effects that stabilizes the tertiary and quaternary structures of proteins. The hydrophobic effect is not due to an intramolecular force but the tendency of hydrophilic and hydrophobic amino acids to interact oppositely with water and segregate into surface and inner regions.
Most proteins can easily dissolve in water Knowing that where within the overal three-dimensional shape of a protein would you most likely find hydrophobic amino acids?
Hydrophobic amino acids are typically found in the interior or core of a protein's three-dimensional structure. This allows them to avoid contact with water molecules and form stable interactions with other hydrophobic amino acids.
What is the resulting amino acid sequence from cgagaaguc?
R E V or Arginine - Glutamic acid - Valine
What type of amino acid side chain would you expect to find on the surface of a protein embedded in a cell membrane?
You would expect to find hydrophobic amino acid side chains on the surface of a protein embedded in a cell membrane. These hydrophobic side chains interact favorably with the hydrophobic lipid bilayer of the membrane, helping the protein to stay anchored in the membrane.
IS VALINE POLAR OR NON-POLAR?
Valine is classified as a non-polar amino acid. Its side chain consists of a branched hydrocarbon structure, which lacks significant electronegative atoms that would create polarity. As a result, valine tends to be hydrophobic and prefers to be found in the interior of proteins, away from the aqueous environment.
Would you find hydrophillic or hydrophobic amino acids on the external surface of a protein a protein?
Hydrophilic amino acids would likely be found on the external surface of a protein as they interact with the aqueous environment surrounding the protein, while hydrophobic amino acids tend to be buried within the protein core away from water.
Are enzymes hydrophilic?
Enzymes, being proteins, are made of many amino acids of which some are hydrophobic. These hydrophobic amino acids tend to shun water and fold into the interior of the protein enzyme. Enzymes are in solution so the hydrophobic sections would be away from the solution on the inside and the hydrophillic amino acids would tend to be on the outside of the enzyme. So, is a limited sense, you could say enzymes are hydrophyllic
What type of interaction would you expect between phenylalanine and leucine in a tertiary structure?
Phenylalanine and leucine are both nonpolar amino acids, so they would likely interact through hydrophobic interactions in the tertiary structure of a protein. These interactions help stabilize the protein's structure by minimizing contact with water molecules.
What amino acids would be most likely found buried deep within the interior of a protein?
Hydrophobic amino acids such as leucine, isoleucine, valine, and phenylalanine are typically found buried deep within the interior of a protein due to their non-polar nature. This helps to maintain the structural integrity of the protein by minimizing interactions with water molecules.
The r group or side chain of the amino acid serine is -ch2-oh the r group or side chain of the amino acid alanine is -ch3 where would you expect to find these amino acids in a globular protein in aq?
Serine, being hydrophilic, will be more likely to appear near the surface of a globular protein in solution, and alanine, being hydrophobic, will more likely appear near the centre of the protein. This illustrates the "hydrophobic effect", which is one of the effects that stabilizes the tertiary and quaternary structures of proteins. The hydrophobic effect is not due to an intramolecular force but the tendency of hydrophilic and hydrophobic amino acids to interact oppositely with water and segregate into surface and inner regions.
Most proteins can easily dissolve in water Knowing that where within the overal three-dimensional shape of a protein would you most likely find hydrophobic amino acids?
Hydrophobic amino acids are typically found in the interior or core of a protein's three-dimensional structure. This allows them to avoid contact with water molecules and form stable interactions with other hydrophobic amino acids.
What is the resulting amino acid sequence from cgagaaguc?
R E V or Arginine - Glutamic acid - Valine
Is water hydrophobic?
no, that would mean water molecules are not attracted to other water molecules
How is it possible for gene with a mutation in coding region to encode a polypeptide with the same amino acid sequence as the nonmutant gene?
If the mutant codon still codes for the same amino acid (a silent mutation). For example: GUU, GUC, GUA and GUG all code for the amino acid Valine. So if the mutation changed the codon from GUU to GUA - Valine would still be produced and therefore the polypeptide will be identical.
If a protein without a hydrophobic domain is synthesized on the rough endoplasmic reticulum's what places would you NOT expect to find it?
If a protein without a hydrophobic domain is synthesized on the rough endoplasmic reticulum, you would not expect to find it integrated into the membrane of the ER, targeted to other membrane-bound organelles, or secreted outside the cell. This is because proteins without hydrophobic regions are less likely to be involved in membrane interactions or secretion pathways.
