BIOL 1201 Chapter : Disulfide Bridges
Document Summary
Sh groups of two cysteine"s form covalent: stabilizes tertiary structure. **which amino acids are found in the interior of a protein?nonpolar. Quaternary structure: multiple polypeptide chains (subunits) fit together to form a larger protein, can be identical subunits or different polypeptide chains. **the sickle-cell hemoglobin mutation alters what level(s) of protein structure? Native and denatured proteins: native-properly folded and functional, denature-unfolded and does not function. Roles of weak bonds in biological systems: easilt made and broken at physiological temperatures, provide specificity, attract and attach substrates to enzymes, determine molecular shape- a compromise between backbone and side groups. If "weak" interactions were "stron" would crystallize the contents of a cell. Small proteins (=peptides) that depress the freezing point of solutions: non-colligative freezing point depression. "hysteresis proteins"- affect freezing point but not the meltion point: decrease the freezing point, do not change melting point, freeze at -2*, melt at . **a colligative property depends on the number of dessiolved molecules true.
