Q.1.
Which of the following is an 8-residue minimal peptide sequence that exhibits intrinsic affinity towards streptavidin and can be fused to recombinant proteins in various combinations?
Q.2.
Strep-tag II hampers protein folding or secretion and it usually interferes with protein function.
Q.3.
Which of the following is a homo-tetramer ofamino acids per subunit?
Q.4.
Strep-tag II is sensitive to cellular proteases.
Q.5.
Streptavidin is naturally secreted by which of the following microorganisms?
Q.6.
An ideal affinity tag should interfere with the folding or bioactivity of a recombinant protein.
Q.7.
Which of the following affinity tag is shown in the figure below?
Q.8.
The affinity of Strep-tag for streptavidin is very high when it is placed at the amino terminus or in between two protein domains.
Q.9.
Which of the following fits in the empty box in the figure below?
Q.10.
Which of the following is used in the column regeneration step of Strep-tag purification, that displaces desthiobiotin?
Q.11.
Which of the following is an engineered streptavidin variant?
Q.12.
Which of the following shows the highest binding affinity for Strep-Tactin?
Q.13.
Which of the following is used in the column regeneration step of Twin-Strep-tag: Strep-Tactin XT purification, that displaces biotin?
Q.14.
Strep-tag I can be used at which of the following positions?
Q.15.
An ideal affinity tag should display an easily controllable binding behavior with sufficient affinity.