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The side chains of some amino acids are hydrophobic but not all. You can see the molecular structure of those that have hydrophobic side chains by going to http://tinyurl.com/ycyj645.
Wiki User
∙ 14y ago
Wiki User
∙ 12y agoA hydrophobic amino acid is an animo acid who's R group is aliphatic or aromatic. This means that the the R groups do not interact well with water and will be buried within the protein.
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What is a non polar amino acid?
Non-polar amino acid is hydrophobic ( GROUP 1)LeucineProlineAlanineValineGlycineMethionineTryptophanPhenylalanineIsoleucine
What is an example of mutation?
The disease sickle cell anaemia occurs due to a mutation. This causes the amino acid glutamic acid (which is hydrophilic) in haemoglobin to be replaced by valine (which is hydrophobic).
How do hydrophobic amino acids and hydrophilic amino acids cause proteind to have a specific shape?
yes
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 is phenolalanine?
DL Phenylalanine is not a vitamin, it is an amino acid. Amino acids are the building blocks of protein. This amino acid, when taken as a supplement, can reduce pain, increase alertness, improve mood and may help Parkinson's disease. My source for this info is 'Prescription for Nutritional Healing" by Phyllis Balch.
What is meant by a hydrophobic amino acid how does it behave around water?
A "hydrophobic" amino acid is an acid that "fears" water. When in contact with water, the hydrophobic amino acid will cause that section of protein to stay away from water.
Is a hydrophobic amino acid?
nope acids are hydophilic.
Is amino acid a hydrophobic substance?
nope acids are hydophilic.
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.
Where in a protein is a hydrophobic amino acid?
in the interior as they are hydrophobic, don't like to have contact with water (hydropyllic,polar)
What is the property of alanine that helps it explain its reaction to water?
The amino acid alanine is non-polar, it has a neutral charge, not positive or negative, and it is hydrophobic.
What is a non polar amino acid?
Non-polar amino acid is hydrophobic ( GROUP 1)LeucineProlineAlanineValineGlycineMethionineTryptophanPhenylalanineIsoleucine
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.
What is an example of mutation?
The disease sickle cell anaemia occurs due to a mutation. This causes the amino acid glutamic acid (which is hydrophilic) in haemoglobin to be replaced by valine (which is hydrophobic).
Why can missenes mutations not have an effect on protein function?
Say the part of the gene that is mutated does not change the amino acid sequence of the protein made through the mRNA; hydrophobic amino acid stays hydrophobic. We have many of these small nucleotide polymorphisms in our genomes and they are useful trackers of human migrations, for instance.
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.
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