ANTH 210 Lecture Notes - Lecture 7: Phenylalanine, Glycosylphosphatidylinositol, Alanine
10 Aug 2018
School
Department
Course
Professor
Document Summary
Lecture 1: introduction to proteins (chapter 3), january 8th 2018. Study of structure, composition, and chemical reactions of substances in living organisms. The cytosol is not empty of packed full of stuff which is mostly proteins. Proteins are made as linear polypeptides by cytosolic ribosomes, but fold into 3-dimensional conformations. Folding provides physical stability and functional surfaces. The sequence of a protein determines its structure, function and localization in the cell. Memorize: structure, name, short abbreviation, and letter abbreviation. Hydrophobic, polar or charged (acidic or basic) Peptide bonds in the backbone are uncharged but polar. Charge and hydrophobicity of a polypeptide is determined by the side chains. Both side chains and backbone can form non-covalent contacts with other amino acids. Peptide bond is planar and cannot rotate. Rotation around the bonds to the central carbon is possible (alpha carbon) Some rotation angles between amino acids in a polypeptide are preferred.
