BB Final Exam--Paper Notes

BB Final - the mutant to slower(but still in increase in rate in the newly engineered protein First Paragraph • Combine experiments with MD

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BB Paper Notes: Introduction: 35-resisdue of HP35 o Small o Ultrafast folding protein Paper solved x-ray structure of HP35 and K24 norleucine (nL) o Atomic resolution o Used laser temp jump to compare folding kinetics Structures are nearly identical to each other—differ from NMR structures previously solved o differences mean a more accurate structure from x-ray crystallography NOT: lattice contacts or crystal/solution differences What do the crystal structures reveal? o Important details of packing of hydrophobic core o Cross-helical H bonds Comparison of crystal structures nL substitution produces only local perturbations The small stabilization by the mutation completely shown in increased rate of folding o SO, mutation suggests that this region of the protein is as structured in the transition state as in the folded structure So, target of engineering to increase the folding rate of the subdomain from faster in
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Unformatted text preview: the mutant to slower (but still in increase in rate) in the newly engineered protein First Paragraph: • Combine experiments with MD simulations of protein folding o Improvement in time resolution for kinetic folding studies Nanosecond optical triggering methods Distributed computing • Can directly MD simulations with experiements on ultrafast folding proteins • Why important: if accurate, contain complete atomic description of the folding mechanism • Computational cost small size and ultrafast folding • HP35 o Subdomain of the headpiece of villin (actin binding protein) o Smallest naturally occurring polypeptide that folds autonomously without any cofactor or disulfide bond Thermostable Globular Hydrophobic core o Resembles...
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This note was uploaded on 12/24/2011 for the course BB 481 taught by Professor Staff during the Spring '11 term at Oregon State.

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