Zusammenfassung der Ressource
Introduction
- Genetics
- 5'-3' orientation
- N terminal --> C terminal
- Protein chains always begin with Met
- Amino acids
- Negative side chains
- Aspartic acid
- Glutamic acid
- Positive side chains
- Arginine
- Lysine
- Histidine
- Uncharged polar side chains
- Asparagine
- Glutamine
- Serine
- Threonine
- Tyrosine
- Nonpolar side chains
- Alanine
- Glycine
- Valine
- Leucine
- Isoleucine
- Proline
- Phenylalanine
- Methionine
- Tryptophan
- Cysteine
- Handedness
- L-type
- CORN crib
- Proteins
- Polymers of amino acid monomers
- Peptide bonds
- Properties
- Shared
- Unique to each amino acid
- Secondary structure
- Alpha helix
- Beta sheet
- Determinants
- Backbone bonds
- Phi angles
- Psi angles
- Hydrogen bonds between main chain atoms
- Supersecondary structure
- The arrangement of
secondary structural regions
- Tertiary structure
- The way in which secondary
structures associate
- Quaternary structure
- The overall protein molecule
- Larger association
- Folding
- Bond types
- Backbone-backbone
- Hydrogen bonds between atoms of two peptide bonds
- Backbone-side chain
- Hydrogen bond between atoms in
peptide bond and amino acid side chain
- Side chain-side chain
- Hydrogen bonds between two
amino acid side chains
- Van der Waals
- Electrostatic attraction
- Structure types
- Transmembrane
- Bacteriorhodopsin
- Globular
- Myoglobin
- Fibrous
- Collagen
- Chaperonins
- Specialised proteins which protect folding
- Cylindrical
- Unfolded protein enters cylinder from one end
- Cap attaches to that end
- Cylinder changes shape
- Hydrohilic environment conducive to folding created
- Properly folded proteins released
- Influences on folding
- Size
- Amino acid content
- Hydrophilic/hydrophobic
- Strength of intramolecular interactions
- Number of S-S bonds
- Domain architecture