BCH210H1 Lecture Notes - Lecture 5: Peptide, Globular Protein, Covalent Bond

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

Document Summary

Globular proteins globular proteins named for their spherical shape. Helices and sheets that make up the core of most globular proteins represents the starting point for protein folding. Hydrophobic core region in which hydrophobic side chains cluster together away from the solvent. Backbone polypeptide backbone itself, excluding side chains. Many proteins exist in nature as oligomers. Oligomer complex composed of often symmetric noncovalent assemblies of two or more monomer subunits. Proteins with two to four subunits predominate in nature subunits of an oligomeric protein typically fold independently and then interact with other subunits. Heterologous interactions involve nonidentical interfaces surfaces are complementary but not symmetric. Denaturation over a small temperature range is evident of a two-state transition between the native and unfolded states of a protein. When weak forces are disrupted at one part of a protein, the entire structure breaks down. Most proteins can be denatured below the transition range by chemical agents.