In this video from the Intel HPC Developer Conference, Erik Lindahl from Stockholm University describes the challenges of cryo-EM, a technique that fires beams of electrons at proteins that have been frozen in solution, to deduce the biomolecules’ structure.
“Structural biology is going through a revolution where cryo-EM now determine 3D structures from 100,000s of noisy images, but it relies on very large computations. I will present our work with Intel to accelerate the RELION program with x86 SIMD, TBB, and MKL to provide outstanding performance.”
Cryo-EM allows molecular samples to be studied in near-native states and down to nearly atomic resolutions. Studying the 3D structure of these biological specimens can lead to new insights into their functioning and interactions, especially with proteins and nucleic acids, and allows structural biologists to examine how alterations in their structures affect their functions. This information can be used in system biology research to understand the cell signaling network which is part of a complex communication system. This communication system controls fundamental cell activities and actions to maintain normal cell homeostasis. Errors in the cellular signaling process can lead to diseases such as cancer, autoimmune disorders, and diabetes. Studying the functioning of the proteins responsible for an illness enables a biologist to develop specific drugs that can interact with the protein effectively, thus improving the efficacy of treatment.
