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Modified from Carley Karsten Lecture 8
Modified from Carley Karsten Lecture 8

... a. primary: amino acid sequence. determined by covalent (peptide) bonds between amino acids. b. secondary: coils and folds. determined by hydrogen bonds between amino and carboxy groups in the backbone. c. tertiary: complex folding. determined by all kinds of bonding between any of the different R g ...
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... tertiary structure and, if applicable, quaternary structure) and how those forces would be affected by the changes in temperature or pH. For example, H bonds, such as in C=O∙∙∙∙H-N, are important in 2°, 3°, and 4° structure. As the temperature of a solution containing the protein is raised, the extr ...
Chapter 1_summary notes
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... polar molecules or ions (e.g. Na+, NO3- etc). Polar substances can form H bonds with polar molecules of water and so dissolve – they are called hydrophilic (water loving) Non-polar substances will not dissolve in water because they cannot form H bonds with water – they are hydrophobic. Rule for subs ...
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... peptides become the outer surface of the surface membrane ...
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... peptides become the outer surface of the surface membrane ...
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... binding domain. The ligand binding domain (LBD) contains a binding site for estrogen. The activity of nuclear receptors is known to be regulated by post translational modifications such as acetylation of lysines and phosphorylation of serines and tyrosines. The LBD (aa 280-502) can be recombinantly ...
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Cyclol



The cyclol hypothesis is the first structural model of a folded, globular protein. It was developed by Dorothy Wrinch in the late 1930s, and was based on three assumptions. Firstly, the hypothesis assumes that two peptide groups can be crosslinked by a cyclol reaction (Figure 1); these crosslinks are covalent analogs of non-covalent hydrogen bonds between peptide groups. These reactions have been observed in the ergopeptides and other compounds. Secondly, it assumes that, under some conditions, amino acids will naturally make the maximum possible number of cyclol crosslinks, resulting in cyclol molecules (Figure 2) and cyclol fabrics (Figure 3). These cyclol molecules and fabrics have never been observed. Finally, the hypothesis assumes that globular proteins have a tertiary structure corresponding to Platonic solids and semiregular polyhedra formed of cyclol fabrics with no free edges. Such ""closed cyclol"" molecules have not been observed either.Although later data demonstrated that this original model for the structure of globular proteins needed to be amended, several elements of the cyclol model were verified, such as the cyclol reaction itself and the hypothesis that hydrophobic interactions are chiefly responsible for protein folding. The cyclol hypothesis stimulated many scientists to research questions in protein structure and chemistry, and was a precursor of the more accurate models hypothesized for the DNA double helix and protein secondary structure. The proposal and testing of the cyclol model also provides an excellent illustration of empirical falsifiability acting as part of the scientific method.
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