Download Aromatic Amino Acids

Survey
yes no Was this document useful for you?
   Thank you for your participation!

* Your assessment is very important for improving the workof artificial intelligence, which forms the content of this project

Document related concepts

Protein purification wikipedia , lookup

Nuclear magnetic resonance spectroscopy of proteins wikipedia , lookup

Western blot wikipedia , lookup

Protein domain wikipedia , lookup

Protein–protein interaction wikipedia , lookup

Protein folding wikipedia , lookup

Protein mass spectrometry wikipedia , lookup

List of types of proteins wikipedia , lookup

Intrinsically disordered proteins wikipedia , lookup

Implicit solvation wikipedia , lookup

Cyclol wikipedia , lookup

Protein wikipedia , lookup

Circular dichroism wikipedia , lookup

Protein structure prediction wikipedia , lookup

Alpha helix wikipedia , lookup

Transcript
Aromatic Amino Acids
Aromatic amino acids are relatively nonpolar. To different degrees, all aromatic amino acids absorb ultraviolet
light. Tyrosine and tryptophan absorb more than do phenylalanine; tryptophan is responsible for most of the
absorbance of ultraviolet light (ca. 280 nm) by proteins. Tyrosine is the only one of the aromatic amino acids with
an ionizable side chain. Tyrosine is one of three hydroxyl containing amino acids.
Least hydrophobic
Very hydrophobic
Aliphatic Amino Acids
Aliphatic R groups are nonpolar and hydrophobic. Hydrophobicity increases with increasing number of C atoms in the hydrocarbon
chain. Although these amino acids prefer to remain inside protein molecules, alanine and glycine are ambivalent, meaning that they can be
inside or outside the protein molecule. Glycine has such a small side chain that it does not have much effect on the hydrophobic
interactions.
The structures below are shown in the ionization state that predominates at pH 7.
Less hydrophobic
More hydrophobic