BCH210H1 Lecture Notes - Lecture 2: Collagen, Hydrophile, Aequorin

• School: UTSG
• Department: Biochemistry
• Course: BCH210H1
• Professor: Stavroula Andreopoulos

Document Summary

Nonpolar amino acids important in the process of folding proteins include all amino acids with alkyl r groups alanine, valine, leucine, isoleucine cyclic structure and aromatic amino acids proline, phenylalanine, tryptophan. Proline is not an amino acids but an -imino acid. Acidic amino acids aspartic acid and glutamic acid contain carboxyl group in r group weaker acids than the. Carboxyl but still exist as coo- at physiological ph and have a net negative charge aspartic acid = aspartate, glutamic acid = glutamate. Proteins that bind metal ions for structure or function contain metal binding sites that contain one or more aspartate or glutamate side chains. Net positive charge at neutral ph histidine, arginine, lysine imidazole group in histidine, guanidino group in arginine, protonated alkyl amino group in lysine. Amino acid hydrophobicity amino acids can be classified as hydrophobic, hydrophilic, or amphipathic. Hydrophobic alanine, glycine, proline, valine, isoleucine, leucine, phenylalanine.