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Biological Membranes

Biological membranes are organized assemblies of lipids and proteins with small
amounts of carbohydrate. Yet they are not impermeable barriers to the passage
of materials. Rather, they regulate the composition of the intracellular medium
by controlling the flow of nutrients, waste products, ions, etc., into and out of the
cell. They do this through membrane-embedded pumps and gates that
transport specific substances against an electrochemical gradient or permit their
passage with such a gradient.
The relative proportions of protein and lipid vary with the type of membrane,
reflecting the diversity of biological roles. For example, certain neurons have a
myelin sheath, an extended plasma membrane that wraps around the cell many
times and acts as a passive electrical insulator. The myelin sheath consists
primarily of lipids, whereas the plasma membranes of bacteria and the
membranes of mitochondria and chloroplasts, the sites of many enzyme-
catalyzed processes, contain more protein than lipid (in mass per total mass).
The boundaries of cells are formed by Biological membranes, the barriers
that define the inside and the outside of a cell.
These barriers prevent molecules generated inside the cell from leaking
out and unwanted molecules from diffusing in; yet they also contain
transport systems that allow specific molecules to be taken up and
unwanted compounds to be removed from the cell. Such transport systems
confer on membranes the important property of selective permeability.
Membranes are dynamic structures in which proteins float in a sea of
lipids. The lipid components of the membrane form the permeability
barrier, and protein components act as a transport system of pumps and
channels that endow the membrane with selective permeability.
In addition to an external cell membrane (called the plasma membrane),
eukaryotic cells also contain internal membranes that form the boundaries
of organelles such as mitochondria, chloroplasts, peroxisomes, and
lysosomes. Functional specialization in the course of evolution has been
closely linked to the formation of such compartments.
Specific systems have evolved to allow targeting of selected proteins into or
through particular internal membranes and, hence, into specific organelles.
External and internal membranes have essential features in common, and these
essential features are the subject of this chapter.
Biological membranes serve several additional important functions
indispensable for life, such as energy storage and information transduction, that
are dictated by the proteins associated with them. In this chapter, we will
examine the general properties of membrane proteins how they can exist in the
hydrophobic environment of the membrane while connecting two hydrophilic
environments and delay a discussion of the functions of these proteins.
Cell adhesion, endocytosis, and the membrane fusion accompanying
neurotransmitter secretion illustrate the dynamic role of membrane proteins.

Fatty acids are carboxylic acids with long-chain hydrocarbon side groups. They
are rarely free in nature but, rather, occur in esterified form as the major
components of the various lipids.The more common biological fatty acids are
listed. In higher plants and animals, the predominant fatty acid residues are
those of the C16 and C18 species palmitic, oleic, linoleic, and stearic acids.
Fatty acids with 14 or 20 carbon atoms are uncommon.
Most fatty acids have an even number of carbon atoms because they are
usually biosynthesized by the concatenation of C2 units.
Over half of the fatty acid residues of plant and animal lipids are unsaturated
(contain double bonds) and are often polyunsaturated (contain two or more
double bonds). Bacterial fatty acids are rarely polyunsaturated but are
commonly branched, hydroxylated, or contain cyclopropane rings. Unusual fatty
acids also occur as components of the oils and waxes (esters of fatty acids and
long-chain alcohols) produced by certain plants.
Fatty acids in biological systems usually contain an even number of
carbon atoms, typically between 14 and 24. The 16- and 18-carbon fatty
acids are most common. The hydrocarbon chain is almost invariably
unbranched in animal fatty acids. The alkyl chain may be saturated or it
may contain one or more double bonds. The configuration of the
double bonds in most unsaturated fatty acids is cis. The double
bonds in polyunsaturated fatty acids are separated by at least one
methylene group.
The properties of fatty acids and of lipids derived from them are markedly
dependent on chain length and degree of saturation. Unsaturated fatty
acids have lower melting points than saturated fatty acids of the same length.
For example, the melting point of stearic acid is 69.6C, whereas that of oleic
acid (which contains one cis double bond) is 13.4C.
The melting points of polyunsaturated fatty acids of the C18 series are even
Chain length also affects the melting point, as illustrated by the fact that the
melting temperature of palmitic acid (C16) is 6.5 degrees lower than that of
stearic acid (C18). Thus, short chain length and unsaturation enhance the
fluidity of fatty acids and of their derivatives.

Saturated fatty acids are highly flexible molecules that can assume a wide range
of conformations because there is relatively free rotation about each of their CC
bonds. Nevertheless, their fully extended conformation is that of
minimum energy because this conformation has the least amount of
steric interference between neighboring methylene groups.
The melting points (mp) of saturated fatty acids, like those of most substances,
increase with molecular mass.
Fatty acid double bonds almost always have the cis configuration. This puts a
rigid 30 bend in the hydrocarbon chain of unsaturated fatty acids that
interferes with their efficient packing to fill space. The consequent reduced van
der Waals interactions cause fatty acid melting points to decrease with their
degree of unsaturation. Lipid fluidity likewise increases with the degree of
unsaturation of their component fatty acid residues. This phenomenon, has
important consequences for membrane properties.
Peptide Classification
Peptide is the name assigned to short polymers of amino acids. Peptides are
classified by the number of amino acid units in the chain. Each unit is called an
amino acid residue, the word residue denoting what is left after the release of
H2O when an amino acid forms a peptide link upon joining the peptide chain.
Dipeptides have two amino acid residues, tripeptides have three, tetrapeptides
four, and so on. After about 12 residues, this terminology becomes cumbersome,
so peptide chains of more than 12 and less than about 20 amino acid residues
are usually referred to as oligopeptides, and, when the chain exceeds several
dozen amino acids in length, the term polypeptide is used.
The distinctions in this terminology are not precise.
Proteins Are Composed of One or More Polypeptide Chains
The terms polypeptide and protein are used interchangeably in discussing single
polypeptide chains. The term protein broadly defines molecules composed of
one or more polypeptide chains. Proteins having only one polypeptide chain are
monomeric proteins. Proteins composed of more than one polypeptide chain
are multimeric proteins. Multimeric proteins may contain only one kind of
polypeptide, in which case they are homomultimeric, or they may be composed
of several different kinds of polypeptide chains, in which instance they are
heteromultimeric. Greek letters and subscripts are used to denote the
polypeptide composition of multimeric proteins. Thus, an type protein is a
dimer of identical polypeptide subunits, or a homodimer. Hemoglobin consists
of four polypeptides of two different kinds; it is an heteromultimer.