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Where would you expect to find a hydrophobic amino acid like valine?
Wiki User
∙ 11y ago
They are found on the inside of the folded chain, away from water. Hydrophobic R groups are nonpolar. By orienting within the folded chain, they avoid coming into contact with water.
Wiki User
∙ 9y ago
Wiki User
∙ 14y agoNo. If the protein is water soluble, you would find mainly hydrophilic R groups
Wiki User
∙ 11y agoin the interior of the folded protein, away from water, or in a transmembrane portion interacting with lipid fatty acid chains
Wiki User
∙ 8y agoThe intramembrane proteins, i.e. the ones that are facing the inner portion of the lipid bilayer, and not the ones facing the cytosol nor the extracellular milieu.
Wiki User
∙ 10y agoOn the inside, away from the water
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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?
hydrophobic, if the protein in the cell membrane is completely in, it means it is hydrophobic, therefore the amino acid chain is also hydrophobic.
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.
Is a mutation dangerous?
Can be, but most mutations are neutral. If you had a gene that coded for a hydrophobic amino acid and it was point mutated to another gene that coded for another hydrophobic amino acid then there would be no change in the protein fold and no danger. Statistically this the the majority of mutation cases.
How many amino acids would you expect to find between the hemoglobin of a human and a wolf?
There are no differences in the amino acids in human hemoglobin and wolf hemoglobin.
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?
leucine
What type of amino acid side chain would you expect to find on the surface of a protein embedded in a cell membrane?
hydrophobic, if the protein in the cell membrane is completely in, it means it is hydrophobic, therefore the amino acid chain is also hydrophobic.
Would you find hydrophillic or hydrophobic amino acids on the external surface of a protein a protein?
Hydrophobic amino acids would be on the external surface of a protein. This is because these are the types of amino acids that help bind things together.
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
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.
What type of interaction would you expect between phenylalanine and leucine in a tertiary structure?
hydrophobic
What would you expect a peptide bond to link to?
two amino cids
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.
An amino acid that is referred to as nonessential would be best described as one that?
A non-essential amino acid is one that the body can produce itself without supplementation and includes Lysine, Leucine, Isoleucine, Methionine, Tryptophan, Theronine, Phenylalanine and Valine.
Is water hydrophobic?
no, that would mean water molecules are not attracted to other water molecules
Is a mutation dangerous?
Can be, but most mutations are neutral. If you had a gene that coded for a hydrophobic amino acid and it was point mutated to another gene that coded for another hydrophobic amino acid then there would be no change in the protein fold and no danger. Statistically this the the majority of mutation cases.
How many amino acids would you expect to find between the hemoglobin of a human and a wolf?
There are no differences in the amino acids in human hemoglobin and wolf hemoglobin.
Which would you expect to have a lower boiling point assuming they were of similar molecular weights a hydrophobic liquid or a hydrophilic one?
hydrophobic would have the lower boiling point as there are less forces of attraction between the molecules. Hydrophilic liquids are polar and therefore have interactions between themselves.
