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The concept of protein energy landscape, focusing on the limitations of protein folding and denaturation. The lecture covers Anfinsen's dogma, the relationship between folding and amino acid sequence, and the impact of external factors on protein trajectories. Topics include thermal instability, denaturation, refolding, and experimental techniques such as X-ray crystallography and protein nuclear magnetic resonance spectroscopy.
Typology: Summaries
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Week 5 Lecture 2
Protein Energy Landscape
What have
we learnt
until now?
01
Limitations
It is not unique. It is not stable
Energy Landscape
Disruption of the native state
Native state or biochemical functional forms may
be disrupted for
● Thermal instability ● High concentrations of solutes ● Inadmissible pH ● Presence of chemical denaturants can do the same
● A fully denatured protein lacks both tertiary and secondary structure, and exists as a so called random coil. ● Mostly denaturation is irreversible. ● Chaperones or heat shock proteins protect against denaturing. ● In some situations some misfolded proteins are unfold, for a second chance to refold properly. This function is crucial to prevent the risk of precipitation into insoluble amorphous aggregates.
Denature, Refolding, Aggregates
Johanna Smriti 19z PSG College of technology