Explore protein evolution in this comprehensive lecture by Lucy Colwell from the International Centre for Theoretical Sciences' Winter School on Quantitative Systems Biology. Delve into the central dogma of molecular biology, amino acid structures, and protein folding mechanisms. Examine advanced techniques like X-ray crystallography and NMR spectroscopy for studying protein structures and dynamics. Investigate the functional effects of mutations, information stored in protein sequences, and methods for extracting useful data from them. Learn about fascinating topics such as the hydrophobic effect, hemoglobin function, and the transplantation of allosteric effects between species. Gain valuable insights into cutting-edge research in protein evolution and its applications in quantitative systems biology.
Protein Evolution and Structure - Lecture 1
International Centre for Theoretical Sciences via YouTube
Overview
Syllabus
Start
Central Dogma: DNA to RNA to Protein
Amino acid structure
Aliphatic and hydrophobic side chains
Definitions of
Antiparallel B-sheet
Energy and forces
Hydrophobic effect
Haemoglobin: carries oxygen from the respiratory organs to the rest of the body.
X-ray crystallography simplified
NMR spectroscopy of proteins protein-lecture googl...
NMR and protein dynamics
How to evaluate the functional effect of mutation?
What information is stored in sequences?
Transplanting a unique allosteric effect from crocodile into human haemoglobin
How to extract useful information from protein sequences?
Taught by
International Centre for Theoretical Sciences
