How is protein structure prediction done in structural proteomics?

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How is protein structure prediction done in structural proteomics?

Protein structure prediction in structural proteomics is typically done using computational methods. These methods utilize various algorithms and techniques to predict the three-dimensional structure of a protein based on its amino acid sequence. The process involves several steps, including sequence alignment, homology modeling, ab initio modeling, and refinement. Sequence alignment is used to identify proteins with known structures that are similar to the target protein, which can provide valuable information for predicting its structure. Homology modeling involves building a model of the target protein based on the known structure of a related protein. Ab initio modeling, on the other hand, predicts the structure without relying on known templates and is based on physical principles and statistical potentials. Finally, refinement techniques are used to improve the accuracy and quality of the predicted protein structure. Overall, protein structure prediction in structural proteomics combines computational methods and available experimental data to generate models that can provide insights into protein function and interactions.