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Why We Like Proteins?

More than 95% of known drug targets are proteins, involved in roughly 93% of drug-target interactions.

But, traditional methods of determining protein structures like the examples given below are extremely expensive and time consuming.

Single Crystal X ray Diffraction 

Approximately
130,000 protein structures determined thus far

Limitations​

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  • Not all proteins can be crystallised; crystallisation is a major bottleneck.

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  • Determining protein structure needs around 100 mg of pure protein and a year of work by a small team.

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  • Lab work is time-consuming.

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  • A protein crystal can yield multiple states of a protein.

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  • Researchers often rely on Argonne National Lab for the Advanced Photon Source.

 

Limitations​

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  • $5M initial capital and $500,000 annual operating costs may be required.

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  • Structure determination of biological macromolecules is limited to large complexes or low-resolution models.

Cryo Electron Microscopy

Approximately 8000 protein structures determined thus far

 

'Nuclear Magnetic Resonance'

Approximately'
14,00 protein structures determined thus far

Limitations​

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  • It is an expensive technique because the protein has to be enriched with radionuclides by feeding 15-N labeled Ammonium Chloride and 13-C labeled Glucose to bacteria.

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  • Variable labeling efficiency.

 

  • Complex NMR spectra for high-molecular-weight biomolecules are challenging to interpret.

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