obtaining a low-to-medium resolution (5–10 Å) reconstruction of the 11 MDa (11,000,000 Da) bacterial flagellar motor obtaining an ultra-high resolution (< 1.5 Å) structure of a drug bound to its protein target identifying the protonation state and the pK$_a$ of a His side chain in an enzyme active site determining whether a protein is intrinsically disordered or contains secondary structure elements
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There are several limiting issues when determining the structures of some proteins. Match each issue with its most appropriate technique (NMR or X-Ray). 1. Nearly any sized protein can be used for this type of structural analysis. 2. Dynamic changes are not easily captured. 3. Smaller proteins are more amenable for this type of structural analysis. 4. Requires isotopic labeling of elements such as N, C, or H. 5. Poorly ordered domains, including disordered domains, will have multiple arrangements averaging out a signal. 6. Large proteins will reorient slowly in solution, averaging out the signal.
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What are the advantages of X-ray crystallography for protein structure determination? a. Novel technique on the cutting edge of protein science b. Good for membrane proteins that are hard to resolve by other techniques c. Able to visualize hydrogens in residues with high resolution, good for smaller proteins d. No size limit; high-resolution structures, well-established technique
Which technique is used to determine structure function relationship in proteins?
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