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Cysteine is considered a polar amino acid because it contains a sulfur atom in its side chain, which can form hydrogen bonds with water molecules. This makes cysteine interact well with water and other polar molecules.

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6mo ago

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Related Questions

Is cysteine a polar amino acid?

Yes, cysteine is a polar amino acid.


Is cysteine a polar or nonpolar amino acid?

Cysteine is a polar amino acid.


Is cysteine a nonpolar amino acid?

No, cysteine is a polar amino acid.


Is cysteine considered a hydrophobic amino acid?

No, cysteine is not considered a hydrophobic amino acid. It contains a thiol group which makes it more hydrophilic.


What amino acids are coded by UGU?

Cysteine ^_^


Is cysteine an essential amino acid in individual consuming diet devoid of methionine?

Cysteine is considered a semi-essential (or conditionally essential) amino acid, meaning that while the body can synthesize it, certain conditions may increase the need for it. In individuals consuming a diet devoid of methionine, which is an essential amino acid and a precursor for cysteine synthesis, the body may not be able to produce sufficient cysteine. Therefore, in such cases, cysteine may be considered essential, as the diet lacks the necessary components for its synthesis.


What type of macromolecule is cysteine?

Cysteine is an amino acid, which is part of the macromolecule protein.


Which amino acid cause curly hairs?

Cysteine.


Is tyrosine a polar or nonpolar amino acid?

Tyrosine is a polar amino acid.


Is tyrosine a polar amino acid?

Yes, tyrosine is a polar amino acid.


What is Crystalline derivative of amino acid cysteine?

The crystalline derivative of amino acid cysteine is N-acetyl-L-cysteine, commonly known as NAC. This compound is a precursor to the antioxidant glutathione and is used in supplements for its antioxidant and mucolytic properties.


Which amino acid is a thiol?

Cysteine is the amino acid that contains a thiol group (-SH) in its side chain. It can form disulfide bonds with other cysteine residues, contributing to protein structure and stability.