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Home >> Industrial and Microbial Biotechnology >> Protein and Enzymes Engineering >>Acquiring knowledge for Protein Engineering Study of Protein Structure Three Dimensional

Acquiring knowledge for Protein Engineering Study of Protein Structure-Three Dimensional
A study of three dimensional structure of a protein (including a study of active sites) is the first step in any exercise on protein engineering. For such a study, protein should be available in crystal form. X-ray diffraction methods have also been developed to generate data at a fast rate, to enable us to predict the three dimensional structure of proteins through model building.

Observed differences in structures of different enzymes can be related with the differences in their function, so that the knowledge from such studies can be used for protein engineering. X-ray diffraction data at different temperatures also allow us to learn, about the changes expected in protein structure due to change in temperature suggesting that protein structure is dynamic. Similarly, NMR (nuclear magnetic resonance) technique will allow us to know the structure of enzymes in solution rather than in crystals, so that we can bypass the time consuming process of crystallization thus speeding up the study of protein structure. The information generated from all these techniques is utilized in protein modeling, which is then utilized for an exercise in protein engineering.

When crystals of a protein are not available for study, but amino acid sequence data is available, the identical sequences in any two proteins are matched and effects of substitution are examined. This is sometimes described as sequence garing and allows us to know which amino acids are involved in catalytic binding at active sites.

 

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