Amino Acids

Phosphorylation caused by kinases, Serine and Threonine kinases and Tyrosine kinases.

Mashup of insertions and deletion, these cause frameshifts.

Change one nucleic base to another

Transitions - Base sequence changes but amino acid product stays the same. Transversion - Base sequence changes and amino acid product changes.

Synonymous (silent) mutation is base sequence changes but still encodes amino acid. Nonsense mutation is base sequence changes and coding codon changes to stop codon. Missense mutation when coding codon is change to a codon for a different amino acid. Conservative - Amino acid is relatively the same, Non conservative - Different size, Charge and Polarity.

Arginine, Histidine, Lysine

Glutamic acid and Aspartic acid

Serine, Threonine, Asparagine, Glutamine, Tyrosine, Cysteine

Glycine, Alanine, Leucine, Isoleucine, Valine, Methionine, Tryptophan, Phenylalaline

Very small R-group

Has 2 rings so large, only AA other than methionine to have only one codon.

R group includes a phenyl ring, very large R-group

Easily interchanged with no effect

1st Amino Acid AUG, contains Sulfur

Ring with NH2 group prevents rotation, found at ends of alpha helices

Terminal SH group allows for disulfide linkages; can hold shape or hold multiple polypeptides together with covalent bond.

Targets of Ser - Thr Kinases; Fairly interchangeable

Target of Tyr-kinases (usually receptor Tyr kinase). Starting material for melanin

Target for N-linked Glycosylation

The AA in RF1 or RF2 that coordinates water molecules for releasing Nascent Polypeptide

Ionizes at physiological pH to have a + charge (salt bridge).

Also ionizes + salt bridge, 6-10 in a row bind tightly to Nickel

Also ionizes + salt bridge, Target of Ubiquitylation

An enzymatic post-translational modification in which a ubiquitin protein is attached to a substrate protein.

Ionizes to form Strong - charge for salt bridges

The AA in RF1 or RF2 that coordinates water molecules for releasing Nascent polypeptide.