front 1 Native Conformation (Protein) | back 1 The folded shape of the protein that is both stable and functional |
front 2 Refolding insulin | back 2 Is 25% but increases to 75% if renatured if chemically cross linked that mimics C chain |
front 3 Hydrophobic core as a determinant of protein folding | back 3 non-polar amino acids want to remain in the hydrophobic core of protein. |
front 4 Helices and sheets as a determinant of protein folding | back 4 Fill space and are hierarchically organized ( folds in a particular order) |
front 5 Surrounding amino acid sequences as a determinant of protein folding | back 5 Insertion of amino acids that should produce a specific 2D structure will not as the other 2D structures effect what that part of the sequence should be |
front 6 X-ray Crystallography | back 6 -need 97% purity -Optimize conditions -Can't do flexible proteins |
front 7 NMR | back 7 - Limit of 35KDa -Can do flexible proteins -need concentrated proteins -2D can analyze proximity of specific amino acids |
front 8 Cyro-Electron Microscopy | back 8 -View in native enviroment - Can't do small over 80KDa -liquid N temp |
front 9 Anfinsen's Experiment | back 9 unfolded proteins can return the their native states |
front 10 Hydrophobic collapse | back 10 Biggest driving force of protein folding |
front 11 Levinthal Paradox | back 11 That proteins fold completely randomly through possible confirmations |
front 12 Stopped Flow Instrument | back 12 Mixes the denatured proteins with the buffer rapidly to kickstart refolding |
front 13 NMR- Pulsed H/D exchange | back 13 Follow as H in protein are exchanged for D in the solvent. Allows for the formation of secondary structure to be viewed |
front 14 1/3 in protein folding pathway | back 14 Hydrophobic collapse -rapid but side chains are still in disarray |
front 15 2/3 in protein folding pathway | back 15 Tertiary structure formation - subdomains folded but not docked together yet, side chains still mobile. |
front 16 3/3 in protein folding pathway | back 16 Final folding -side chain forms final conformation, remaining water is expelled |
front 17 Landscape Theory | back 17 polypeptides fold through various conformational adjustments that reduce free energy state until reaching their native state. (Funnel) |
front 18 Paper Chromatography | back 18 stationary is cellulose based paper and the mobile phase is a solvent more or less polar, Molecules seperated based on polarity |
front 19 Thin Layered | back 19 silica gel on glass or plastic plate with a mobile phase of a more or less polar solvent. |
front 20 Hydrophobic Interactions | back 20 Stationary phase is hydrophillic lightly substitued with hydrophobic groups which during the mobile phase will attract the protein. Will be eluted by salt gradient |
front 21 Reverse Phase | back 21 The stationary phase is a non polar liquid subbed with n-alkyl chains the mobile phase is a polar solvent. Seperation is by hydrophobic forces by solute and ligands |
front 22 Dialysis | back 22 Rebuff of the protein. With a semipermable memberane allow for the excess solvent and protein to reach equilimbrium |
front 23 Ultrafiltration | back 23 Used to rebuff protein sample or to concentrate the sample. Loose leaf tea basket cup but spin it and toss the tea (buffer) |
front 24 Ultracentrigution | back 24 seperate heavy particles by spinnn |
front 25 Zonal Centrigfution | back 25 Sep according to sedimentry coeffecient and fraction out the results |
front 26 Equilimbrium density centrigfution | back 26 Separation by the density of the particles from a uniform solution, form bands in their isopycnic positions |
front 27 Western Blotting | back 27
|