Exam 20: Designer Proteins and Protein Folding

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Adding restriction sites when constructing plasmids will help with _______.

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Using site-directed mutagenesis, the mutation of a serine residue to an alanine residue might be used to _________. I. decrease the solubility of a protein II. eliminate the possibility of phosphorylation at that location III. observe the impact of a non-polar side chain at that location IV. prove that serine had a catalytic function in the native protein V. promote proper folding of the protein

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Which statement is true about SPPS:

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Unfolded (denatured) proteins can be re-folded by removing the chemicals in a process called _________.

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Levinthal's conclusion was that protein folding _______, because it would take way too long to complete the folding if all randomly available rotations around the main chain bonds would be sampled to achieve the most stable structure.

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Protein engineering is possible because of advances in biochemistry and molecular biology. Various _______ in a protein sequence are _____ in order to determine the role they played in the protein.

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Plasmids are _________. They can be delivered into the cell by ______ or _______.

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Proteins can be denatured using β\beta -mercaptoethanol, since this reagent will _____________.

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During protein folding the entropy of the solvent molecules _______.

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Given a peptide: Given a peptide:   Hydrogen bonds will form in this peptide in a buffer at pH 7 between: Hydrogen bonds will form in this peptide in a buffer at pH 7 between:

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Proteins can be synthesized in the lab by using ____________. I. solid-phase peptide synthesis (SPPS) II. protein overexpression in biological systems (cells) III. esterification reactions IV. polymerization reactions V. hydrolysis reactions

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Given a peptide: Given a peptide:   Salt bridges will form in this peptide in a buffer at pH 7 between: I. the amino terminus -NH<sub>3</sub><sup>+</sup> and the carboxy terminus -COO<sup>-</sup> II. the side chain of Asp6 and the amino terminus -NH<sub>3</sub><sup>+</sup> III. the side chains of Ser6 and Gln9 IV. the side chain of His13 and the carboxy terminus -COO<sup>-</sup> V. the side chains of Gln9 and His13 Salt bridges will form in this peptide in a buffer at pH 7 between: I. the amino terminus -NH3+ and the carboxy terminus -COO- II. the side chain of Asp6 and the amino terminus -NH3+ III. the side chains of Ser6 and Gln9 IV. the side chain of His13 and the carboxy terminus -COO- V. the side chains of Gln9 and His13

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What are the disadvantages of studying proteins in their purified form?

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The origin of replication enables the plasmid to ______________.

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__________ suppression is used to incorporate unnatural amino acids into a protein using cellular expression.

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Engineered proteins can be expressed in a variety of host cells (mammalian, bacterial, etc). Choosing the host cell depends on ___________.

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Molecular dynamics simulations can be used to model the sequence in which the _____ structure of a protein forms during protein folding.

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Whistleblowers are in general protected from being fired from the job by __________.

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The ___________ sequence is needed to predict the 3D structure of a relatively small protein using de novo structure prediction software.

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The amine group of the amino acid monomers used in SPPS can be protected by a ____________. I. phosphate group II. tert-butoxycarbonyl group (t-Boc) III. fluoprenylmethyloxycarbonyl group (Fmoc) IV. sulfonamide group

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