Biological Membranes Flashcards

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1
Q

Membranes

A

barrier surrounding cells and membranous organelles - but allow selective transport between compartments.
Receive extracellular signals which influence gene expression.
Anchorage points for structures, both inside the cell (cytoskeleton) and outside (extracellular matrix; other cells). (Lecture 6&7)
site for specialised enzyme function (e.g. mitochondrion or chloroplast).

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2
Q

Functions

A

Boundary and Permeability
Organisation and localisation
Transport processes
Nutrients
Signal
Cell-cell processing

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3
Q

Phospholipid bilayer

A

Permeable to hydrophobic molecules
Permeable to small, uncharged molecules
Very low permeability/not permeable to large, uncharged molecules
Not permeable to charged ions

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4
Q

Components

A

The lipid content is largely made up of phospholipids which are Amphipathic
This means molecules with a polar (hydrophilic) head and a non-polar (hydrophobic) tail

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5
Q

The chemical properties of water impact molecular interactions in cells

A

Hydrophilic head group
backbone (e.g. glycerol)
Hydrophobic carbon tail
Molecule is always amphipathic

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6
Q

Phospholipid backbone

A

Phospholipids constructed from a glycerol backbone are called phosphoglycerates
Examples: phosphatidylcholine (most common), phosphatidylserine, phosphatidylethanolamine….
The head group.

glycerol

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7
Q

Sphingosine

A

backbone in sphingomyelin – rich in myelin

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8
Q

Most phospholipids have the glycerol backbone

A

Sphingomyelin is the exception.

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9
Q

What happens if you mix water with uncharged (hydrophobic) molecules?

A

favorable interactions – a cage-like structure forms around it

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10
Q

Why do phospholipid bilayers form?

A

Bilayer formation is energetically favorable.
Hydrophilic head interact with water.
Hydrophobic tails are in contact with each other

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11
Q

Factors

A

Temperature
The nature of the phospholipids (Phosphatidylcholine, Phosphatidylinositol etc.)
The amounts of saturated and unsaturated fatty acids.
The presence of cholesterol or other sterols

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12
Q

Excitable Membranes

A

Excitable Membranes

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13
Q

The outer Carbohydrate layer

A

Glycoproteins - short oligosaccharide chain (3-10)
Proteoglycans – one/more polysaccharide chain (>10)
Cells have an outer sugar coating – ‘carbohydrate layer’
Protective – sugar attracts water – slimy layer that protects and helps motion
Cell-cell recognition

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14
Q

Sugars=Simple Carbs

A

Composed entirely of carbon, hydrogen and oxygen: CnH2nO
Form rings or linear strands
Monosaccharides,
disaccharides,
oligo-, poly-saccharides

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15
Q

Membranes also have carbohydrates on the outer surface that serve as recognition sites for other cells and molecules

A

Glycolipids—carbohydrate + lipid

Glycoproteins—carbohydrate + protein

Adding carbohydrate moieties (Glyco…

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16
Q

Membrane Asymmetry

A

The two leaflets of a membrane are not identical. Each may contain different types of phospholipid and a different arrangement of proteins and carbohydrates.
The two sides of the membrane may have different functions

17
Q

Double bonds make a kink – influence fluidity

A

Double bond in unsaturated tail makes kinks in the tail
Gaps caused by kinks in plasma membrane filled with cholesterol
High cholesterol levels makes membranes more rigid.

18
Q

Peripheral

A

Can be attached to an integral membrane protein
Attachments are temporarily:
Hydrophobic interaction
Electrostatic interaction
Non-covalent interactions
Easily removed from the cell membrane

19
Q

Integrtal

A

Transmembrane proteins extend all the way through the phospholipid bilayer.
Permanently embedded – can only remove with detergent
They have one or more transmembrane domains:
Transmembrane domains are usually composed of a-helices
Hydrophilic amino acids are internalised
Hydrophobic amino acids are on the outside in contact with the lipid bilayer

20
Q

Lipid anchored

A

covalently attached to lipid bilayer and are referred to as anchored membrane proteins
These lipid anchors include long-chain acyl or prenyl groups, glycosyl-phosphatidylinositol (GPI) and cholesterol.
The lipid association with proteins can be either reversible or irreversible and an individual protein may have more than one lipid anchor attached.