Q. There are a large number of protein folds available, compared to millions of protein sequences.

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Q. In Rosetta, The segments with assigned _______ structures are subsequently assembled into a ______ dimensional configuration.

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Q. Rosetta is a web server that predicts protein three-dimensional conformations using the ab initio method.

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Q. Searching for a fold with the absolute minimum energy may not be valid in reality.

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Q. The prediction programs are thus designed using the energy minimization principle.

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Q. Which of the following is untrue about Ab initio prediction?

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Q. Energy minimization has to be used with caution because excessive energy minimization often moves residues away from their correct positions.

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Q. In the step of Model Refinement Using Energy Function, the structural irregularities can be corrected by applying the energy minimization procedure on the entire model, which moves the atoms in such a way that the overall conformation has the lowest energy potential.

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Q. In Side Chain Refinement step, A side chain can be built by searching every possible conformation at every torsion angle of the side chain to select the one that has the lowest interaction energy with neighboring atoms.

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Q. Which of the following is untrue about specialized programs for loop modeling?

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Q. The procedure begins by measuring the orientation and distance of the anchor regions in the stems and searching PDB for segments of the same length that also match the above endpoint conformation.

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Q. Which of the following is untrue about Loop Modeling Step?

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Q. Which of the following is untrue about Backbone Model Building Step?

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Q. Which of the following is untrue about Sequence Alignment Step?

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Q. Which of the following is untrue about template Selection Step?

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Q. Which of the following is untrue about homology modeling?

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Q. Jpred combines the analysis results from six prediction algorithms, including PHD, PREDATOR, DSC, NNSSP, Jnet, and ZPred.

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Q. Prof is not similar to PHD.

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Q. Which of the following is untrue regarding PSIPRED?

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Q. Leucine zipper domains are a special type of coiled coils found in transcription regulatory proteins which contain two anti parallel α-helices held together by hydrophobic interactions of leucine residues.

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