Key Area 3 Flashcards
Integral membrane proteins:
Interact with the hydrophobic tail of phospholipids in membrane to hold it in the bilayer.
Some are transmembrane proteins.
Transmembrane proteins.
When integral protein spans the entire width of the membrane.
E.g. Channels, transporters and receptors
Peripheral membrane proteins.
Have hydrophilic R groups on their surface.
Bound to the surface of membranes by ionic and hydrogen bonds.
Many interact with the surfaces of integral membrane proteins.
The phospholipid bilayer:
Barrier to ions and most uncharged polar molecules.
Small molecules (oxygen, carbon dioxide) pass through the bilayer by simple diffusion.
Facilitated diffusion:
The passive transport of substances across the membrane through specific transmembrane proteins.
To perform specialised functions:
Different cell types have different channel and transporter proteins.
Channel proteins:
Highly selective.
Multi-subunit proteins.
Subunits arranged to form water-filled pores across the membrane.
Some are gated and change conformation to allow or prevent diffusion.
Ligand-gated channels:
Controlled by the binding of signal molecules.
Voltage-gated channels:
Controlled by changes in ion concentration.
Transporter proteins:
Bind to the specific substance to be transported.
Undergo a conformational change to transfer substance across the membrane.
Alternate between two conformations so that the binding site is sequentially exposed on both sides of the bilayer.
Active transport:
When protein pumps transfer substances across the membrane against their concentration gradient.
Requires metabolic energy (ATP).
Protein pumps:
Transporter proteins coupled to an energy source.
ATPases:
Protein pumps that hydrolyse ATP to provide the energy for the conformational change.
Electrochemical gradient:
Formed from the concentration gradient and the membrane potential.
Determines the transport of the solute.
Membrane potential
Electrical potential difference.
Created when there is a difference in electrical charge on the two sides of the membrane.