Protein structure and function 2 Flashcards
Quaternary structure
number and arrangement of multiple folded protein subunits in a multi-subunit complex
can be simple dimers to oligomers
Bonds between subunits in quaternary structure
normally interact non-covalently, can have disulfide bonds
contain closely packed non-polar side chains, H bonds between backbones and side chains
Spatial arrangement of quaternary structure
polypeptide subunits associate with specific geometry
Types of proteins
fibrous and globular
Fibrous proteins
normally display one type of secondary struture
Globular proteins
exhibit regular secondary structure interspaced with stretches devoid of recognisable structure
Example of globular protein
haemoglobin
Haemoglobin structure
4 globin subunits adult: 2α and 2β subunits fetal: 2α and 2γ subunits one haem group per subunit binds to O2 deoxyHB subunits held together by salt bridges and H bonds
How does O2 binding affect the structure of Hb?
conformational change, subunit-subunit salt bridges break, H-bonding changes, weaker interaction between αβ dimers
Co-operativity of haemoglobin
deoxyhaemoglobin has relatively low affinity for O2, but when one O2 molecule binds to one haem group, affinity for 2nd O2 to bind is increased
Structure of transmembrane proteins
span membrane with a stretch of hydrophobic amino acids
Role of protein modifications
regulation of protein activity: phosphorylation, methylation, acetylation
regulation of destination: lipidation, glycosylation
Glycosylation
attachment of carbohydrates
particularly for extracellular and cell-surface proteins
in euks: aids folding of protein, role in cell-to-cell recognition (aid in targeting and trafficking of newly synthesised protein to its destination)
How do some diseases/disorders arise in relation to proteins
misfolding: can act as seeds for aggregation
Example of disease
prion diseases
result from misfolding and aggregation of Celluar Prion Protein
early symptom of toxicity: activation of immune response causing inflammation