Shown at the right is the structure of serine. These amino acids are usually found at the surface of proteins, as discussed in the Proteins 2 module. These are serine (Ser), threonine (Thr), cysteine (Cys), asparagine (Asn), glutamine (Gln), and tyrosine (Tyr). Six amino acids have side chains that are polarīut not charged. This fact has important implications for proteins' tertiary structure (see the Proteins 2 module for a discussion of tertiary structure). These side chains are composed mostly of carbon and hydrogen, have very small dipole moments, and tend to be repelled from water. Shown at the right is the structure of valine. Side chains are glycine (Gly), alanine (Ala), valine (Val), leucine (Leu), isoleucine (Ile), proline (Pro), phenylalanine (Phe), methionine (Met), and tryptophan (Trp). protein found in the plaques of Alzheimer disease. The nine amino acids that have hydrophobic Peptides of alternating hydrophilic and hydrophobic amino acid residues have a tendency to adopt. Amino acids are grouped according to what their side chains are like.
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