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a) Self-replication.
b) Storing and transmitting information.
c) Maintaining selectively dierent environments
(transport; cell signalling and
compartmentalization).
d) Harnessing and transforming energy.
Non-Covalent Bonds
a) Substantial number -
Determined by chemistry of the
molecule i.e. charge and bond
polarity.
b) Surface topography that
interacting surfaces to
approach each other closely - Cholesterol Membrane Proteins
complementary shapes.
Normal temp. - reduced Transporters
fluidity - ID-ID between Receptors
Spontaneous Assembly of Bilayer
ring and tails. Enzymes
a) Shape of phospholipids. Low temp. - increased Anchors - Cell structure and shape.
b) Amphipathic nature. fluidity - prevents tight
c) Hydrophobic eect. packing.
Roles of Proteins
As enzymes.
For movement or locomotion e.g. the flagellum.
For transport e.g. active transport, facilitated transporters.
For structure or adhesion e.g. cytoskeleton proteins.
As signalling proteins.
Secondary Structure - Local 3D structure stabilized by hydrogen bonding in the backbone of the polypeptide.
Tertiary Structure - Overall 3D structure formed by folding of entire polypeptide, stabilized by interactions between R
groups (non covalent interactions and disulfide bonds) as well as interactions between R groups and the backbone
atoms. [multiple alpha helices and beta barrels (beta sheets twisted & coiled to form a closed structure) are tertiary]
Quaternary Structure - 3D arrangement of two or more polypeptides, interacting to form a protein complex
composed of multiple subunits.
Denaturation
pH - aects ionization state of ionic amino acids.
Temperature - heat breaks down non-covalent interactions.
Detergents - bind to protein and destabilize non-covalent interactions.