Question
The X-ray crystallographic analysis of a protein often fails to reveal the positions of the first few and/or the last few residues of a polypeptide chain. Explain.
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The crystal causes a beam of incident X-rays to diffract into many specific directions. Show more…
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Our growing understanding of how proteins fold allows researchers to make predictions about protein structure based on primary amino acid sequence data. Consider the following amino acid sequence. (FIGURE CAN'T COPY) (a) Where might bends or $\beta$ turns occur? (b) Where might intrachain disulfide cross-linkages be formed? (c) Assuming that this sequence is part of a larger globular protein, indicate the probable location (external surface or interior of the protein) of the following amino acid residues: Asp, Ile, Thr, Ala, Gln, Lys. Explain your reasoning. (Hint: See the hydropathy index in Table 3-1.)
(a) For many years it was difficult to determine the X-ray structures of proteins that are imbedded in membranes because, when they are extracted into an aqueous buffer, they denature. Explain why this denaturation occurs. (b) In some cases, this denaturation can be prevented by extraction of the protein from the membrane with detergents (Sec. 20.5). Explain.
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