BIOLOGY 151 Lecture Notes - Lecture 27: Beta Sheet, Alpha Helix, Tyrosine Kinase
Document Summary
Use this to decide which amino acids would be found on the inside/outside of the protein. Glycine is not really all that nonpolar just has a hydrogen. Tyrosine has a benzene ring which is hydrophobic, but because it has an oh it can be considered polar or hydrophilic. Tyrosine kinase put phosphate on tyrosine of another protein (means more likely to be on outside, not going to go digging on inside to add phosphate to another) Primary structure- amino acid sequence in the protein. If we say the primary structure is changed, this means the amino acid sequence in the protein is changed, usually by a mutation. Secondary structure- consists of beta pleated sheets or alpha helices. The things holding alpha helices and beta pleated sheets together is hydrogen bonds between backbones. Quaternary structure- multiple polypeptides making up a protein.