Protein functions commonly rely on conformational changes within the protein. Extensive conformational changes are associated with protein folding immediately during or after their synthesis in vivo, when they fold to acquire their native conformational structure. Knowledge of the location of functionally relevant conformational changes within the protein and the magnitude and rates of conformational interconversion among various protein conformations (i.e. dynamics) are of great importance to the understanding of protein function.
Reference
Artigues, A., Nadeau, O. W., Rimmer, M. A., Villar, M. T., Du, X., Fenton, A. W., & Carlson, G. M. (2016). Protein structural analysis via mass spectrometry-based proteomics. Advances in Experimental Medicine and Biology, 919, 397–431. https://doi.org/10.1007/978-3-319-41448-5_19
Sample 1:
Specific function of proteins depends on their structure and orientation. Analysing the changes in the structure gives insights into its role. (Artigues et al 2016)
Reference
Artigues, A., Nadeau, O. W., Rimmer, M. A., Villar, M. T., Du, X., Fenton, A. W., & Carlson, G. M. (2016). Protein structural analysis via mass spectrometry-based proteomics. Advances in Experimental Medicine and Biology, 919, 397–431. https://doi.org/10.1007/978-3-319-41448-5_19
Q: Sample 1 utilises the case in accordance with best academic integrity practices
- A. True
- B. False
