BIO 201 Lecture Notes - Lecture 4: Globin, Peptide, Protein Structure

• School: University at Buffalo
• Department: Biological Sciences
• Course: BIO 201
• Professor: Lara Hutson

Document Summary

Levels of protein structure (cont. : tertiary structure, quaternary structure. Carbohydrates: monosaccharide structure, polymerization and disaccharides, polysaccharides: starch, glycogen, & cellulose. Tertiary (3 ) structure: * complete 3d structure of a polypeptide (usually * also involves r-group interactions) They do(cid:374)"t like to (cid:271)e e(cid:454)posed, alwa(cid:455)s (cid:272)up to the i(cid:374)terior. Quaternary (4 ) structure: * interactions between polypeptides: multi-subunit* proteins only. Homomultimers: comprised of two or more identical polypeptide subunits. Heteromultimers: comprised of two or more different types of polypeptide subunits. Properly folded protein -> unfolded change in 1 degree structure -> toxic protein clump. Caused by a mutation: 1 amino acid changed in -globin. Common in regions where malaria is widespread. Changed to 1 degree structure changed to 3 degree and 4 degree structure. Native protein (active) -> boil(disrupts all non-covalent interactions)-> denatured protein (inactive) [ cool, renatured protein] or [ interactions between inappropriate side chains aggregated clumps inactive and possible toxic]