Please enable JavaScript.
Coggle requires JavaScript to display documents.
Proteins - Coggle Diagram
Proteins
Non-Covalent interactions
Hydrogen Bonds -
extremely important for structure
Hydrophobic Interactions -
often drive protein folding
Electrostatic Bonds -
Protein stability
van der Waals forces -
Protein stability
Secondary Structure -
Structure is mantained by h-bonds between amide H and carboxyl O
Alpha-helix
Beta-sheet
Types of protein conformations
Integral -
Embedded within membrane -> cannot be released by changing pH or salt concentration
Lipid Anchored
Peripheral -
Globular proteins -> electrostatic and H bonds for interactions
Primary Structure
(linear) -> covalent bonds
Nucleotide Sequence
Tertiary Structure -
Stabilised by side chain interactions of non-neighbouring amino acids
Beta-globin polypeptide
Protein Types
Fibrous - Tend to be structural ->
Bone and connective tissue
Globular -
most proteins are globular -> usually water-soluble
Domains
Proteins < 250 AA have a simple, compact globular shape
Large globular proteins are typically made up of multiple recognizable and distinct structures ->
domains
consist of a single continuous portion of the protein sequence
domain sequence can be interrupted by a sequence belonging to another part of the protein
Supersecondary Structures
Motifs -
grouping of secondary structures
Quaternary Structure -
Multi-subunit Protein
Hemoglobin Molecule
Helix-breakers ->
Proline
Helix-formers -
most amino acids
random coil ->
Asparagine, Serine
Indifferent ->
Glycine