BCH 100 Final: Learning objectives 5: Proteins 2 (Explained)

• School: UC Riverside
• Department: Biochemistry
• Course: BCH 100
• Professor: Stephanie Dingwall

Document Summary

Lecture 5: protein structure and function 2: terminology: subunit, denaturation (and denaturant), ligand, prosthetic group, fractional saturation, cooperativity, binding site, allosteric (allosteric site, allosteric regulator, allosteric regulation) A single protein that associates with other proteins to form a whole. (usually quaternary structure) Inactivation of a protein by loss of the structural order (2 , 3 , 4 , or a combination of these) Source that causes denaturation: heat, changes in ph, detergents (sodium dodecyl sulfate (sds)), urea/guanidine, -mercaptoethanol (disrupts disulfide bonds). Small molecule bound by protein tightly-bound non-protein part of protein. For each successive o2 bound, the binding of the next. For example, 2,3-bisphosphoglycerate stabilizes t-state by binding to pocket in hb that exists only in the t-state. Regulation: molecule binds to a site other than the active site to change activity of protein. Learning objectives: describe the general structure (arrangement of hydrophobic vs. polar r groups) of a globular protein that is embedded in a lipid bilayer (membrane).