exam_scoop_tut10

exam_scoop_tut10 - Classification or clustering of protein...

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Picture 1 Tutorial 10 2010 4 20 14:12
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Picture 2 2 i oxygen negative charge: i& , stability steric hindrance --> affect beta sheet Change to serene much smaller, but still -ve clashes
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Picture 3 Picture 4 Picture 5 Picture 6 Picture 7 Picture 8 Picture 9 **change rotamer: #2 is the best one. activity P172S Proline: cis [most peptide bonds are trans!!] Mutate: must change to trans. Folding of the strand will be different. Next to active site: Anything that mutates --> reduce enzymatic efficiency! --> disease phenotype R393H/G i& H Bond!!! Destabilized protein! G488S Glycine is flexible Serine will rigidify the protein! Examination Scope 2010 4 20 14:54
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Property of each group of amino acids (hydrophobic/ acidic) How peptide bonds are formed How the get into formation of alpha helices and beta sheets
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Unformatted text preview: Classification or clustering of protein families and subfamilies Experimental methods of (NMR and X-ray crystallography) Similarities of How they will result in the structures. How to judge the quality of structures done by NMR/X-ray (given structure, how would u determine if it is good/bad model, what parameters will u look at) o X-ray: R-factors, R plots, bond length/angle deviations (~asgn1) o NMR: ___________? How would you do protein modeling. How do u judge if the protein you generate is reasonable or not (~asgn2) must not be experimental! Non-protein ligand interaction [CD38]. What sorts of interaction. What can u tell? What can u proceed to do? That math -_-! Structural difference of protein VS disease...
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exam_scoop_tut10 - Classification or clustering of protein...

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