Membrane Protein

General functions of membrane

protein

Passage of nutrients into cell & metabolic out of it

Maintain ionic composition and pH of cytosolic

Anchoring points for many of the cytoskeletal fibers

thatpermeate the cytosol, imparting shape and strength to cells

Bind signaling molecules (e.g., hormones, growth factors,

neurotransmitters)

Enzyme, intracellular signal transducers, and stabilizing the

membrane

Form specific junctions between cells to strengthen tissues

Type of membrane protein

Integral membrane proteins (transmembraneproteins)

Lipid-anchored membrane proteins

Peripheral membrane proteins

Integral membrane proteins

Has three domains : cytosolic, exoplasmic, and membranespanning domain

The cytosolic and exoplasmic domains have hydrophilic exterior

surfaces

The membrane-spanning domain contains manyhydrophobic

amino acids that interact with the hydrocarbon core of the
phospholipid bilayer

The membrane-spanning domains consist of one or more

alphahelices or of multiple beta strands

Integral membrane proteins

Most transmembrane proteins (exoplasmicdomains) are

glycosylated

Asymmetricallyoriented (binds with carbohydrate chain) =

glycoprotein

Example: antigens of human ABO blood group

The mobility is restricted by interactionswith the rigid

submembrane cytoskeleton

Examples of integral membrane protein : glycoporin,

bacteriorhodopsin, and porin

Features in Glycoporin

A typical singlepass transmembrane protein

Extracellulardomain -heavily glycosylated

Membrane embedded hydrophobic side chains from alpha helix

form van der waals interactions with the fatty acyl chains

Form coiled-coil dimer

Positively chargedarginine and lysine bind with

negativelycharged phospholipid head groups to help anchor
glycophorin in the membrane

Structure of Glycoporin

Feature in Bacteriorhodopsin

A multipass transmembrane protein

Has seven hydrophobic alpha helices

A protein found in the membraneof certain photosynthetic

bacteria

Help bacteria to synthesize ATP with help of light

Another examples of multipass transmembrane protein:

G-protein-coupled receptors cell signaling
Ion channels (tetrameric proteins) regulate ion flows

Structure of Bacteriorhodopsin

Feature in Porin

Structure differs radically from that of other integral proteins

Trimers of identical subunits; each subunit, 16 beta-strands

form a barrel-shaped structure with a pore in the center

Unlike a typical water-soluble globular protein, aporin has a

hydrophilic inside and a hydrophobic exterior

Several types of porin are found in the outer membrane

of gram-negative bacteria such as E. coli and in the outer
membranes of mitochondria and chloroplasts

Structure of Porin

Lipid-anchored membrane
proteins

Bound covalentlyto one or more lipid molecules

The hydrophobic carbonchain of the attached lipid is embedded in

one leaflet of themembrane and anchors the protein to the
membrane

Thepolypeptide chain itself does not enter the

phospholipidbilayer

Divided into:

Acyl anchor

Prenyl anchors

GPI anchors

Type of Lipid-anchored membrane

proteins

Lipid-anchored membrane
proteins

Acyl anchor: A group of cytosolic proteins are anchored to the

cytosolic face of a membrane by a fatty acyl group (e.g.,
myristateor palmitate) attached to the N-terminal glycine
residue

Prenyl anchors:A second group of cytosolic proteins are

anchored tomembranes by an unsaturated fatty acyl group
attached toa cysteine residue at or near the C-terminus

GPI anchors:Some cell-surface proteins and heavily glycosylated

proteoglycans of the extracellular matrix are bound to the
exoplasmic face of the plasma membrane by a third type of
anchor group, glycosylphosphatidylinositol (GPI)

Peripheral membrane proteins

Do not interact with thehydrophobic core of the phospholipid

bilayer

Instead theyare usually bound to the membrane indirectly by

interactionswith integral membrane proteins or directly by
interactionswith lipid head groups

Localized toeither the cytosolic or the exoplasmic face of the

plasmamembrane

The exoplasmic domains of integral membrane proteins are often

attached to components of the extracellular matrix orto the cell
wall surrounding bacterial and plant cells