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Chapter 8 – Structure description. Venn diagram. Structures. Coordinates. Alpha or beta coordinates. Distance matrices. Handedness. Torsion angles. Ramachandran plot. Protein secondary structures.
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Chapter 8 – Structure description Chapter 8. Strucure description
Venn diagram Chapter 8. Strucure description
Structures Chapter 8. Strucure description
Coordinates Chapter 8. Strucure description
Alpha or beta coordinates Chapter 8. Strucure description
Distance matrices Chapter 8. Strucure description
Handedness Chapter 8. Strucure description
Torsion angles Chapter 8. Strucure description
Ramachandran plot Chapter 8. Strucure description
Protein secondary structures • Globular proteins which are solvable, packs the hydrophobic side chains inside the molecule. This makes a hydrophobic kernel and hydrophilic surface. • The backbone is polar, hence hydropholic. To neutralize this hydrophility there are hydrogen bindings between NH and CO on the backbone. • This is done by constructing regular secondary structures • Helices, alpha most usual • Beta sheets • They are made by succeeding residues having equal torsion angles Chapter 8. Strucure description
Alpha helix Chapter 8. Strucure description
Beta sheets Chapter 8. Strucure description
DSSP – Define Secondary Structure of Proteins • DSSP identifies both the SSEs and solvent exposure of proteins.It is mainly based on H-bond patterns, and must therefore include a method for identifying those. Chapter 8. Strucure description
Determining helices Chapter 8. Strucure description
Determining beta strands Chapter 8. Strucure description
Structure comparison Chapter 8. Strucure description
Requirement for structure descriptions Chapter 8. Strucure description
Desribing structure pieces Chapter 8. Strucure description
Space based description Chapter 8. Strucure description
Framework for pairwise structure comparison Chapter 8. Strucure description
Cannot use pure dynamic programming for structure comparison Chapter 8. Strucure description