BIOS 4630 Lecture Notes - Lecture 5: P53, Bohr Effect, Hemeprotein
26 Jan 2017
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Protein unfolding (protein denaturation: what denatures proteins, proteins are only marginally stable, urea (non-covalent bonds)- strong denature attacks a variety of bonds, heat (disrupts h bonds, detergents (disrupt hydrophobic, extreme ph (disrupts salt bridges) Protein folding: why fold, g= h-t s, g<0, g>0, but s, s= sfinal-sintital, smyoglobin=+170 (j/kmol), there is an overall increase in entropy, energy landscape of protein folding/misfolding. Some diseases involving protein (mis)folding: cataracts (a-crystallin, cystic fibrosis (cftr, cancer (p53, prion diseases, alzhei(cid:373)er"s, parki(cid:374)so(cid:374)"s, hu(cid:374)ti(cid:374)gto(cid:374)"s, type ii diabetes. Ad (cid:894)alzhei(cid:373)er"s disease(cid:895) i(cid:374) ge(cid:374)eral populatio(cid:374: 5. 3 million affected in u. s ( billion, without a breakthrough, it is expected that by 2050 up to 15 million will be. Vi. affected in us: by 2040, china will have more patients with dementia than developing countries combined. How does protein structure and properties relate to function: myoglobin (mb, hemoglobin (hb) Nobel laureates 1962: john kendrew (mb, max perutz (hb)
