Amino Acids Lippincott Chapter 1: Nanuka Tsiklauri, MD

Amino Acids
Lippincott chapter 1
NANUKA TSIKLAURI, MD.
OVERVIEW
 Proteinsare the most abundant and functionally diverse
molecules in living systems.
 Virtually every life process depends on this class of molecules.
 proteins
display an incredible diversity of functions, yet all share
the common structural feature of being linear polymers of amino
acids.
 proteinshave unique three-dimensional structures, making them
capable of performing specific biologic functions.
STRUCTURE OF THE AMINO ACIDS
 Although more than 300 different amino acids have been described in
nature, only 20 are commonly found as constituents of mammalian
proteins.
 Each amino acid (except for proline, which has a secondary amino group)
has a carboxyl group, a primary amino group, and a distinctive side
chain (“R-group”) bonded to the α-carbon atom.
 At physiologic pH (approximately pH 7.4), the carboxyl group is
dissociated, forming the negatively charged carboxylate ion (–COO⎺), and
the amino group is protonated (–NH3⁺).
 In proteins, almost all of these carboxyl and amino groups are combined
through peptide linkage and, in general, are not available for chemical
reaction except for hydrogen bond formation
Classification
 Thus, it is the nature of the side chains that ultimately dictates the
role an amino acid plays in a protein.
 classify the amino acids according to the properties of their side
chains, that is, whether they are nonpolar (have an even distribution
of electrons) or polar (have an uneven distribution of electrons, such
as acids and bases;
Nonpolar amino
acids
Each amino acid is shown in its
fully protonated form, with
dissociable hydrogen ions
represented in red print.
The pK values for the α-

carboxyl and α-amino groups of
the nonpolar amino acids are
similar to those shown for
glycine.
Amino acids with nonpolar side chains
 Each of these amino acids has a nonpolar side chain that does not gain or lose protons or
participate in hydrogen or ionic bonds
 The side chains of these amino acids can be thought of as “oily” or lipid-like, a property that
promotes hydro phobic inter – actions
 In proteins found in aqueous solutions––a polar environment––the side chains of the
nonpolar amino acids tend to cluster together in the interior of the protein.
 This phenomenon, known as the hydrophobic effect, is the result of the hydro phobicity of
the nonpolar R-groups, which act much like droplets of oil that coalesce in an aqueous
environment.
 The nonpolar R-groups thus fill up the interior of the folded protein and help give it its three-
dimensional shape.
 However, for proteins that are located in a hydrophobic environment, such as a membrane,
the nonpolar R-groups are found on the outside surface of the protein, interacting with the
lipid environment
Location of nonpolar amino acids
in soluble and membrane proteins.
Proline
 Proline differs from other amino acids in that proline’s side
chain and α-amino N form a rigid, five-membered ring
structure
 Proline, then, has a secondary (rather than a primary) amino
group.
 It is frequently referred to as an imino acid.
 The unique geometry of proline contributes to the formation of
the fibrous structure of collagen, and often interrupts the α-
helices found in globular proteins.
Amino acids with uncharged polar side
chains
 These amino acids have zero net charge at neutral pH, although
the side chains of cysteine and tyrosine can lose a proton at an
alkaline pH.
 Serine, threonine, and tyrosine each contain a polar hydroxyl
group that can participate in hydrogen bond formation
 The side chains of asparagine and glutamine each contain a
carbonyl group and an amide group, both of which can also
participate in hydrogen bonds.
Amino acids with acidic side chains
 The amino acids aspartic and glutamic acid are proton donors.
 At physiologic pH, the side chains of these amino acids are fully ionized, containing a
negatively charged carboxylate group (–COO⎺).
 They are, therefore, called aspartate or glutamate to emphasize that these amino acids are
negatively charged at physiologic pH.
Amino acids with basic side chains
 The side chains of the basic amino acids accept protons.
 At physiologic pH the side chains of lysine and arginine are fully ionized
and positively charged.
 In contrast, histidine is weakly basic, and the free amino acid is largely
uncharged at physiologic pH. However, when histidine is incorporated into
a protein, its side chain can be either positively charged or neutral,
depending on the ionic environment provided by the polypeptide chains of
the protein.
 This is an important property of histidine that contributes to the role it plays
in the functioning of proteins such as hemoglobin
Optical properties of amino acids
 The α-carbon of an amino acid is attached to four different chemical groups and is, therefore,
a chiral or optically active carbon atom.
 Glycine is the exception because its α-carbon has two hydrogen substituents and, therefore,
is optically inactive.
 Amino acids that have an asymmetric center at the α-carbon can exist in two forms,
designated D and L, that are mirror images of each other
 The two forms in each pair are termed stereoisomers, optical isomers, or enantiomers.
 All amino acids found in proteins are of the L-configuration.
 However, D-amino acids are found in some antibiotics and in plant and bacterial cell walls.
Essential Amino Acids
 All 20 types of amino acids are required for protein synthesis. These amino acids can be
derived from digesting dietary protein and absorbing their constituent amino acids or,
alternatively, by synthesizing them de novo.
 There are 10 amino acids that cannot be synthesized in humans and thus must be provided
from dietary sources. These are called the essential amino acids.
 Arginine is required only during periods of growth or positive nitrogen balance
Hydrophobic amino acids
• Phenylalanine and tyrosine are precursors for catecholamines.

• Tryptophan can form serotonin and niacin.
• Valine, leucine, and isoleucine are branched-chain amino acids whose
metabolism is abnormal in maple syrup urine disease
• Proline is a secondary amine whose presence in a protein disrupts normal
secondary structure.
Hydrophilic amino acids
• Have side chains that contain O or N atoms; some of the hydrophilic side chains
are charged at physiologic pH
• The acidic amino acids (aspartic and glutamic acids) have carboxyl groups that
are negatively charged, whereas the basic amino acids (lysine, arginine, and
histidine) have nitrogen atoms that are positively charged.

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Amino Acids

The pK values for the α-

• Phenylalanine and tyrosine are precursors for catecholamines.

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