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Haixu Tang School of Inforamtics
Protein structures Haixu Tang School of Inforamtics
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A covalent peptide bond
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Protein conformation is specified by tts Amino Acid sequence
Steric interactions Weak non-covalent bonds hydrogen bonds ionic bonds van der Waals attractions Hydrophobic interaction distribution of its polar and nonpolar amino acids
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Protein folding: lowest energy conformation
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Protein denaturalization
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Visualizing protein conformations
Protein structures in atomic level Protein Data Bank (PDB) Pymol: Rasmol:
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Protein secondary structure
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Secondary structure prediction
Prefer a-helix: Ala, Leu, Met, Phe, Glu, Gln, His, Lys, Arg (sidechains cover and protect the backbone H-bonds) Prefer b-sheet: Tyr, Trp, Phe, Ile, Val, Thr, Cys (large bulky sidechains) Disrupt secondary structure: Gly, Pro, Ser, Asp, Asn (small, restrained, or sidechain hydrogen bonds)
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Coiled coil
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Protein Domains Independent structural unit Independent function
Independent folding Independent evolve
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Protein families
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Class Folds Super-families Families
Protein structural classification (SCOP: Class Folds Super-families Families
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Sulfur-sulfur (disulfur) bonds
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Assembly of Large Structures
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Experimental determination of protein structures
X-ray crystallography NMR (Nuclear Magnetic Resonance) Spectroscopy
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X-ray crystallography
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NMR spectrum
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