BIOL130 Study Guide - Protein Folding, Chronic Obstructive Pulmonary Disease, Heat Shock Protein
20 Nov 2014
School
Department
Course
Professor
Document Summary
Proteins, the most versatile macromolecules, are absolutely vital to human life (di guisepp, 2001). A protein is made up of amino acid subunits, and has a primary structure of an amino acid chain and a secondary structure in which there are beta pleated sheets and alpha helixes coiling the primary structure. The secondary structure then folds into the tertiary structure, where there are side chain interactions such as covalent bonds and weak intermolecular forces (di guisepp, 2001). Proteins can unfold, or change their 3-d shape, becoming denatured. Once denatured, some proteins can spontaneously refold while others need aid (di guisepp, 2001). Molecular chaperones are proteins which help other proteins fold, either in their initial folding (cotranslation), or after they have become denatured (hartl, 1996). Molecular chaperones prevent protein aggregation, or clumping, which allows the protein to fold without interacting with other proteins (hartl, 1996).
