LESSON 13: PROTEINS

Proteins
• Derived from the Greek word proteios, meaning “first.”
• All proteins in humans are polymers made up from 20
different amino acids.
• We can function well with the presence of proteins,
enables transport of various food materials, homeostasis
or can act as an antibody
• Each kind of protein is composed of amino acids
arranged in a specific order that determines the
characteristics of the protein and its biological action.
• Proteins provide structure in membranes, build cartilage
and connective tissue, transport oxygen in blood and
muscle, direct biological reactions as enzymes, defend the
body against infection, and control metabolic processes
as hormones.
• They can even be a source of energy.
• The different functions of proteins depend on the
structures and chemical behavior of amino acids, the
building blocks of proteins.
Amino Acids
• Carboxylic acid group (COOH)
• Amino group (NH2)
• Hydrogen atom (H)
• Side Chain (R)
• Amino acids differ on their “R” group
Solubility of Protein as affected by pH
• At low pH's, proteins have a net positive charge because
the amide gains an extra proton.
• At high pH's, they have a net negative charge due to the
carboxyl on the protein backbone losing its proton.
• At their pI (isoelectric point) value, a protein has no net
charge.
• This leads to reduced solubility because the protein is
unable to interact with the medium and will then fall out
of solution.
Isoelectric Point
• Zwitterion state changed when conditions are varied
• The pH at which a particular molecule or surface carries
no net electrical charge
• when pH is lowered, the charges are dominated by
negative charged particle, which will repel the charges,
causing insolubility
• Ex. When milk spoils, curd forms due to the change in
pH (acidic) which changes the charge of the proteins,
repelling the charges of whey and milk proteins.

Properties of Amino Acids

(1) CRYSTALLINITY AND SOLUBILITY
• amino acids are white crystalline substances
• Soluble to some extent in water but which are mostly
insoluble in organic solvents (polarity)

(2) AMPHOTERIC
• the combination of an amino group and a carboxyl group
in the same molecule results in it being to act as an acid
or base.

(3) IONIC CHARACTER

• It contains a (+) and a (-) group
• Amino acids are weak electrolytes, and they ionize
according to the pH of the system
• Thus, if acid is added to a neutral solution of an amino
acid, a (+) ion is formed, whereas, if alkali is added a (-)
ion is formed.
• ZWITTERION - a chemical compound that is electrically
neutral but carries formal positive and negative charges
Ionization of Amino Acids
• Although we have drawn an amino acid with uncharged
amino (-NH2) and carboxylic acid (-COOH) groups, these
groups are ionized for amino acids in most body fluids.
• At physiological pH, the –NH2 group gains H+ to give its
ionized form –NH3+ and the –COOH group loses H+ to give
its ionized form COO
• An ionized amino acid which has both a positive charge
and a negative charge, is a dipolar ion called a zwitterion.

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LESSON 13: PROTEINS
• In the zwitterion, the ionized regions have charge POLAR
balance, which means that the ionized amino acid has an ‣ Serine ‣ Cysteine
overall zero charge.
‣ Threonine ‣ Asparagine
• As zwitterions, amino acids are similar to salts. Thus,
Tyrosine ‣ Glutamine
amino acids have high melting points and are soluble in
water, but not in organic solvents. ACIDIC BASIC
‣ Aspartic Acid ‣ Histidine
Classification of Amino Acids ‣ Glutamic Acid ‣ Lysine
• We can now classify amino acids using their specific R ‣ Arginine
groups, which determine their characteristics in aqueous
solution.

(3) NON-ESSENTIAL AMINO ACIDS

• The amino acids in which the body can synthesize for
itself.
• Proteins in foods usually deliver these amino acids, but
(1) NONPOLAR AMINO ACIDS it is not essential that they do so.
• Have hydrogen, alkyl, or aromatic R-groups, which make • The body can make all nonessential amino acids, given
them hydrophobic (water fearing). nitrogen to form the amino group and fragments from
• Amino Acids: carbohydrate or fat to form the rest of the structure.
‣ Glycine ‣ Alanine ‣ Valine • Amino Acids:
‣ Leucine ‣ Isoleucine ‣ Phenylalanine ‣ Alanine ‣ Glutamine
‣ Methionine ‣ Proline ‣ Tryptophan ‣ Arginine ‣ Glycine
‣ Asparagine ‣ Proline
‣ Aspartic Acid ‣ Serine
‣ Cysteine ‣ Tyrosine
‣ Glutamic Acid

(4) ESSENTIAL AMINO ACIDS

• There are nine amino acids that the human body either
cannot make at all or cannot make in sufficient amount to
meet its needs.
• Amino Acids:
‣ Phenylalanine ‣ Histidine
(2) POLAR AMINO ACIDS
‣ Valine ‣ Arginine
• have R groups that interact with water, which makes
‣ Tryptophan ‣ Lysine
them hydrophilic (water loving).
‣ Threonine ‣ Leucine
• The polar neutral amino acids contain hydroxyl thiol or
‣ Isoleucine
amide (-CONH2) groups.
• The R group of a polar acidic amino acid contains a
Formation of Peptide Bond
carboxylate (-COO) group.
• A peptide bond is an amide bond that forms when the -
• The R group of a polar basic amino acid contains a
COO- of one amino acid reacts with -NH3+ of the next
nitrogenous or amino group (NH2), which ionizes to give
amino acid
an ammonium ion.
• The linking of two or more amino acids by peptide bonds
forms a peptide

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LESSON 13: PROTEINS
• Two amino acids form a dipeptide, three forms tripeptide,
four forms tetrapeptide, five is a pentapeptide, and long
chains of amino acids form polypeptide
• 50 or more amino acids is classified as a protein not a
polypeptide
Naming Peptides
• With the exception of the C terminal amino acid, the
names of all other amino acids in a peptide end with -yl.
• Ex. A tripeptide consisting of alanine at the N terminal,
glycine, and serine at the C terminal is named as one word,
alanylglycylserine
• For convenience, the order of amino acids in a peptide
is often written as the sequence of three-letter
abbreviation.
• free ammonia group is N terminal while free carboxyl
groups are C terminals
*CONCEPT CHECK*
• Consider the dipeptide Val-Pro
VALINE (a) What amino acid is the N terminal
amino acid?
PROLINE (b) What amino acid is the C terminal
amino acid?
PEPTIDE BONDS (c) How are the amino acid
connected?
VALYLPROLINE (d) Give the name of the dipeptide
PROLYLVALINE (e) Give the name of the dipeptide in
which the amino acid order is
reversed as Pro-Val?
Levels of Protein Structure
• When there are more than 50 amino acids in the chain,
the polypeptide is usually called a protein.
• Each protein in our cells has a unique sequence of amino
acids that determines its biological function
• more peptide, more complex the structure
(1) PRIMARY STRUCTURE
• basic structure of protein with 50 amino acids
• simple chain
• Particular sequence of amino acids held together by
peptide bonds.
• Amino acid sequence within protein varies.
‣ Ex. A hormone that stimulates the thyroid to release
thyroxin is a tripeptide with amino acid sequence Glu-
His-Pro
▪ Although other amino acid sequences are
possible, such as His-Pro-Glu or Pro-His-Glu, they
do not produce hormonal activity.
▪ Thus, biological function of peptides and proteins
depends on the sequence of amino acids
*CONCEPT CHECK* – Primary structure
Val-Val-His-Pro What are the abbreviations of the
possible tetrapeptide containing two
valines, one proline, and one histidine
if the C terminal is proline?
(2) SECONDARY STRUCTURE
• longer and more amino acid units
• more amino acid units, the structure is more
compressed (and shorter) due to pleating or curves,
causing carboxylates and amino groups to interact
• Determined by weak electrical attractions within the
polypeptide chain.
• Describes a type of structure that forms when amino
acids formed by the attraction of positively charged
hydrogen to the nearby negatively charged oxygen with a
polypeptide or between polypeptides.
• The three most common types of secondary structure
are the alpha helix, beta pleated sheet, and triple helix
(a) ALPHA HELIX (α-helix)
• Hydrogen bonds form between the oxygen of the
C=O groups and the hydrogen of N-H groups of
the amide bonds in the next turn of the α-helix.
• Because there are many hydrogen bonds along
the polypeptide, it has a helical shape of a spiral
staircase.
• The R groups of the different α amino acids
extend to the outside of the helix.
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LESSON 13: PROTEINS
(b) BETA PLEATED SHEET (β-pleated sheet)
• Hydrogen bonds form between the oxygen
atoms in the carbonyl groups of one polypeptide
chain and hydrogen atoms in the N-H groups of
the amide bonds in adjacent polypeptide chains.
‣ As a result, several polypeptide chains are
held together side by side like folded or pleated
sheets

(c) TRIPLE HELIX

• Collagen, which is the most abundant protein in
the body, makes up 25-35% of all proteins in
vertebrates.
• Found in connective tissue, blood vessel, skin,
tendons, ligaments, the cornea of the eye, and
cartilage
• Its strong structure is a result of three α helical
polypeptides woven together like a braid to form
triple helix.
Types of R-group Interactions
(a) Hydrophobic interactions are interactions between
two non-polar R groups. Within a protein, the amino
acids with non-polar R groups move away from
aqueous environment to form a hydrophobic center
at the interior of the protein molecule.

(3) TERTIARY STRUCTURE

• Involves attractions and repulsions between the R
groups of amino acids in the polypeptide chain.
• As interactions occur between different parts of the
peptide chain, segments of the chain twist and bend until
the protein acquires a specific three-dimensional shape.
• Stabilized by interactions between the R groups of the
amino acid in one region of the polypeptide chain and the
R groups of amino acids in other regions of protein.
(a) GLOBULAR PROTEINS (b) Hydrophilic interactions are interactions between the
• Have a compact, spherical shapes because external aqueous environment and the R groups of
sections of the polypeptide chain fold over on top polar amino acids moving the polar amino acids
of each other due to various interactions between toward the outer surface of globular proteins where
R groups. they form hydrogen bonds with water.
• globe-like shape
• It is the globular protein that carry out the work
of the cells: functions such as synthesis, transport,
and metabolism
• Myoglobin is a globular protein that stores
oxygen in skeletal muscle.
• High concentrations of myoglobin are found in
the muscles of sea mammals, such as seal and
whales

(b) FIBROUS PROTEINS

• Proteins that consist of a long, thin, fiber-like
shapes.
• They are typically involved in the structures of (c) Salt bridges are ionic bonds between ionized R
cells and tissues groups of basic and acidic amino acids. (strong bond)
• Two types of fibrous protein are α-keratins and • Ex. Ionized R group of arginine, which has a
β-keratins. positive charge, can form a salt bridge (ionic bond)
• α-keratins are proteins that make up hair, wool, with the R group in aspartic acid, which has a
skin and nails (consist of α-helix structure that negative charge.
coils together by disulfide bond)
• Β-keratin found in feathers of birds and scales of
reptiles (consist of β-pleated sheet structures

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LESSON 13: PROTEINS
(d) Hydrogen bonds form between H of a polar R group
and the O or N of another amino acid.
• Ex. Hydrogen bond can form between the –OH
groups of two serine’s or between the –OH of
serine and –NH2 in the R group of glutamines.
(e) Disulfide bonds (-S-S-) are covalent bonds that form
between the –SH groups of cysteines in a polypeptide
chain. Strong type of bond which renders the heat
stability of some proteins.
(4) QUATERNARY STRUCTURE
• if the primary, secondary and tertiary structures are
combined it results to a quaternary structure
• In the quaternary structure, the subunits are held
together by the same interactions that stabilize tertiary
structures, such as hydrogen bonds, salt bridges,
disulfide links, and hydrophobic interactions between the
R groups.
• Each subunit of the hemoglobin contains a heme group
that binds oxygen
*CONCEPT CHECK*
Indicate which of the following are present in the (1)
primary, (2) secondary, (3) tertiary, (4) quaternary or (5)
all levels of structures of protein:
5 (a) Peptide bonds
2 (b) Hydrogen bonds between adjacent peptides
2 (c) Hydrogen bonds within a single peptide
3 & 4 (d) Hydrophobic interactions
4 (e) Association of four polypeptide chains
Denaturation of Proteins
• weakening of the bonding, loosening of coiled structures
• primary structure is not affected by denaturation (unless
enzymatic means)
• an irreversible process
• Occurs when there is a change that disrupts the
interaction between R groups that stabilize the secondary,
tertiary and quaternary structure, that is they uncoil and
lose their shapes and consequently lose their ability to
function.
• However, the covalent amide bonds of the primary
structure are not affected.
• The loss of secondary and tertiary structures occurs
when conditions change, such as increasing the
temperature or making the pH acidic or basic.
• Past a certain point, denaturation is irreversible.
‣ Ex. Hardening of egg when it is cooked, curdling of
milk when it is acidified, stiffening of egg whites when
they are whipped.
‣ In the body, proteins are denatured when they are
exposed to stomach acid.
‣ Whipping of egg whites in meringue preparation
disrupts the protein structures (agitation)
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LESSON 13: PROTEINS
Solubility of Simple Proteins
(1) ALBUMINS – soluble in water & neutral salt
solution; precipitated by saturation with
((NH4)2SO4)
(2) GLOBULINS – soluble in neutral salt solution such
as NaCl and sparingly soluble in water.
Precipitated by one-half saturation with
(NH4)2SO4 and by saturation with NaCl
Types of Proteins
(3) GLUTELINS – Insoluble in water and dilute
(1) SIMPLE PROTEINS
solutions of neutral salts, but soluble in dilute acid
• Gives amino acid residues upon hydrolysis
and alkali
• Ovalbumin in egg whites
(4) PROLAMINES – Soluble in 60-80% ethanol
• Gliadin in wheat
insoluble in water
• Zein in corn
(5) PROTAMINES – soluble in water, dilute acid, and
• Collagen
ammonia
• Myosin
(6) SCLEROPROTEINS – insoluble in water, dilute
solutions of neutral salts, acid and alkali and 60-
ALBUMIN GLOBULIN GLUTELIN
80% ethyl alcohol.
• blood • blood (serum • wheat (glutenin) (7) HISTONES – soluble in water and dilute acid and
(serumbumin) globulins) • rice (oryzenin)
insoluble in ammonia; contain large quantities of
• milk • potato (tuberin)
(lactalbumin) • Brazil nuts
lysine and arginine. Histones are often combined
• egg white (excelsin) with nucleic acids
(ovolbumin) • lentils (legumin)
• lentils • Globular tertiary (2) CONJUGATED PROTEINS
(legumelin) protein structure • Proteins containing other moieties
• kidney beans • SP + Fat → Lipoprotein
(phaseolin) • SP + Dye → Chromoprotein
• wheat (leucosin).
• Globular tertiary
• SP + CHO → Glycoprotein
protein structure • SP + Metals → Metalloprotein
PROLAMINE PROTAMINE HISTONE • SP + Phosphate groups → Phosphoprotein
• wheat and rye • sturgeon • Thymus gland, • Non-protein components are called prosthetic groups
(gliadin) (sturine) pancreas, • Ovomucoid in egg whites
• corn (zein) • mackerel nucleoproteins • Casein (phosphoprotein)
• rye (secaline) (scombrine) (nucleohistone). • Nucleoproteins (DNA, RNA)
• barley (hordein). • salmon (salmine) • yields large • Heme (metalloprotein)
• high in amide • herring amounts of lysine
nitrogen and (clapeine) and arginine (3) DERIVED PROTEINS
proline • strongly basic, • combined with
• Altered proteins
• occurs in grain high in arginine, nucleic acids
• Produced from partial hydrolysis via chemical or
seeds. associated with within cells
DNA enzymatic methods
• Types of derived proteins
Scleroproteins are connective tissues and hard tissues.
Simple and fibrous protein; insoluble in all solvents and PRIMARY SECONDARY
resistant to digestion. • Slightly modified • Extensively modified
COLLAGEN ELASTIN KERATIN • Insoluble in water • genetic means
Connective Elastin: Ligaments, Hair, nails, hooves, • Ex. rennet coagulated • does not coagulate in
tissues, bones, tendons, and horns, and protein, cooked egg, heat
cartilage, and arteries. Similar to feathers. Partially cooked custard • Arranged in order of
gelatin. Resistant collagen but resistant to increasing solubility
to digestive cannot be digestive enzymes; ‣ Proteose
enzymes but converted to contains large ‣ Peptone
altered to digest gelatin. amounts of sulfur, ‣ Peptides
gelatin by boiling as cystine
• Molecular weight is
water, acid, or
alkali; high in
inversely related to
hydroxylproline. solubility
Relevant in the textures of meat (toughening or soft)

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