Biology 1002B Lecture Notes - Lecture 3: Western Blot, Northern Blot, Rhodopsin
31 May 2016
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For a protein to be functional : it must fold correctly (primary tertiary) Anfensen"s dogma: polypeptide must fold into native 100% active tertiary protein, add a denaturant such as urea (polar molecule, disrupts h bonding, replace urea with buffer, refold the native confirmation (>90% active) Primary sequence is only thing that is needed and that tertiary folding depends on. Macromolecular crowding (in vivo) can interfere with protein folding: in vitro (in test tube) 0. 1mg/ml, in vivo (in a cell) - >300mg/ml. Chaperones: interacts with and stabilizes non-native forms of protein. Looks like a bottle where protein goes inside: not part of the final assembly of proteins, requires energy (atp, needed due to the large amount of proteins in a cell. What drives protein folding: levinthal paradox (don"t need to know) Given a small protein of 100 amino acids. If each residue can assume three different conformations, the total number of structures would be 3100 which is equal to.
