NE224 Lecture Notes - Lecture 7: Christian B. Anfinsen, X-Ray Crystallography, Groel
9 Oct 2014
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Document Summary
Protein structures can be determined at atomic resolutions by x-ray crystallography and nmr: Crystal structures usually represented by a single model. Note: the structure is not rigid, in solution (and crystal) there are always fluctuations in the structure over time, i. e. proteins are dynamic. Nmr structures represented by a family of models. Figure 8-38b the 2d proton nmr structures of proteins. (b) the nmr structure of a 64-residue polypeptide comprising the src protein sh3 domain. The information specifying how a protein folds from an extended chain to its native structure is contained in its. Ribonuclease a: denature rnasea in 8m urea and -mercaptoethanol. Remove urea by dialysis (see ch 6) Often proteins do not fold or refold efficiently. Other proteins can promote folding: (i) (ii) (iii) protein disulfide isomerases: assist in forming correct disulfide bonds proline cis-trans isomerases: accelerate slow interconversion of cis and trans conformations or peptide bonds involving pro (v&v fig.
