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Proteins

This document discusses proteins and amino acids. It begins by defining proteins as polypeptides consisting of amino acids joined by peptide bonds. There are 20 common amino acids that serve as the building blocks of the thousands of diverse proteins found in nature. The structure of a typical amino acid contains an alpha carbon bonded to an amino group, carboxyl group, hydrogen, and a variable side chain. Proteins can be classified based on their structural shape as either fibrous or globular proteins, or based on their composition as simple proteins or conjugated proteins containing other groups. The 20 common amino acids are also discussed, including their 3-letter and 1-letter codes, structures, and classifications based on properties like hydrophobicity.

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0% found this document useful (0 votes)
23 views29 pages

Proteins

This document discusses proteins and amino acids. It begins by defining proteins as polypeptides consisting of amino acids joined by peptide bonds. There are 20 common amino acids that serve as the building blocks of the thousands of diverse proteins found in nature. The structure of a typical amino acid contains an alpha carbon bonded to an amino group, carboxyl group, hydrogen, and a variable side chain. Proteins can be classified based on their structural shape as either fibrous or globular proteins, or based on their composition as simple proteins or conjugated proteins containing other groups. The 20 common amino acids are also discussed, including their 3-letter and 1-letter codes, structures, and classifications based on properties like hydrophobicity.

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NOTES on PROTEINS

Dr. Gyebi A. G
Biochemistry Department
Bingham University Karu.

Proteins (Greek proteios, ―primary‖ or ―of first importance‖) are biochemical molecules
consisting of polypeptides joined by peptide bonds between the amino and carboxyl groups of
amino acid residues.
The repeating units in peptide is called amino acid residue. Proteins are polypeptides that are
made up of 40-100 amino acids

Proteins are the indispensable agents of biological function, and amino acids are the building
blocks of proteins. The stunning diversity of the thousands of proteins found in nature arises
from the intrinsic properties of only 20 commonly occurring amino acids. These features include
(1) the capacity to polymerize, (2) novel acid–base properties, (3) varied structure and chemical
functionality in the amino acid side chains, and (4) chirality.

The structure of a single typical amino acid is shown in Figure 1. Central to this structure is the
tetrahedral alpha (α) carbon (C), which is covalently linked to both the amino group and the
carboxyl group. Also bonded to this -carbon is a hydrogen and a variable side chain (R). It is
the side chain, the so called R group that gives each amino acid its identity. It is sufficient for
now to realize that, in neutral solution (pH 7), the carboxyl group exists as -COO- and the amino
group as -NH3+. Because the resulting amino acid contains one positive and one negative charge,
it is a neutral molecule called a zwitterion. Amino acids are also chiral molecules. With four
different groups attached to it, the -carbon is said to be asymmetric. The two possible
configurations for the -carbon constitute non identical mirror image isomers or enantiomers.
Figure: 1 Structure of an Amino Acid Skeleton
A. Amino acids share Common structural features.
i. C atom center, Amino group on one side carboxylic acid on the other, and an R group that can
be H or more complicated will explore in a minute.
ii. 20 common AA called standard AA’s other AA‘s derived from these AA‘s usually by post-
translational modification (ie AA was changed after it was made into a protein)
iii. All 20 AA‘s have trivial names
All have a 3 letter code
All have a 1 letter code
I expect you to know codes and structures for all AA‘s
Naming substituents on AA‘s is not standard organic chem. base C is called alpha C then out
from there is beta, gamma, delta, epsilon.
iv. All AA‘s expect Glycine are chiral.
All AA‘s expect Glycine have 4 different constituents around Cá.
Why is this important?
Chiral center non-superimposable mirror images enantiomers optically active
(Will rotate plane polarized light and display differential absorbtion of circularly polarized light)

Classification of proteins by Structural Shape


Proteins can be classified on the basis of their structural shapes:
• Fibrous proteins are made up of long rod-shaped or stringlike molecules that can intertwine
with one another and form strong fibers.
– insoluble in water
– major components of connective tissue, elastic tissue, hair, and skin
– e.g., collagen, elastin, and keratin.
• Globular proteins are more spherical in shape
– dissolve in water or form stable suspensions.
– not found in structural tissue but are transport proteins, or proteins that may be moved easily
through the body by the circularoty system
– e.g., hemoglobin and transferrin.
Classification by Composition
Proteins can also be classified by composition:
• Simple proteins contain only amino acid residues.
• Conjugated proteins also contain other organic or inorganic components, called prosthetic
groups.
– nucleoproteins — nucleic acids (viruses).
– lipoproteins — lipids (fibrin in blood, serum lipoproteins)
– glycoproteins — carbohydrates (gamma globulin in blood, mucin in saliva)
– phosphoproteins — phosphate groups (casein in milk)
– hemoproteins — heme (hemoglobin, myoglobin, cytochromes)
– metalloproteins — iron (feritin, hemoglobin) or zinc (alcohol dehydrogenase).
Symbols of Amino acids
Amino Acid 3-Letter 1-Letter
Leucine Leu L
Lysine Lys K
Methionine Met M
Phenylalanine Phe F
Proline Pro P
Serine Ser S
Threonine Thr T
Tryptophan Trp W
Tyrosine Tyr Y
Valine Val V
Alanine Ala A
Arginine Arg R
Asparagine Asn N
Aspartate Asp D
Cysteine Cys C
Histidine His H
Isoleucine Ile I
Glutamine Gln Q
Glutamate Glu E
Glycine Gly G
CLASSIFICATION OF AMINO ACIDS
Amino-Acids Classification Based on Standard and NonStandard Amino Acids
1. Standard amino-acids: Those 20 amino acids are encoded by universal genetic code
2. Non-Standard amino-acids: Two amino acids incorporated into proteins by unique
synthetic mechanism
•Selenocysteine: Incorporated when mRNA translated included SECIS (selenocysteine
insertion seq) element, causes the UGA codon to encode selenocysteine instead of stop
codon)
•Pyrrolysine: used by methanogenic archaea in enzyme that they use to produce
methane. It is coded for UAG stop
Standard amino acids
•All proteins are composed of the 20 ―standard "amino acids.
•Common central alpha (α)-carbon atom bound to a carboxylic acid group, an amino group and a
hydrogen atom are covalently bonded.
•They have a primary amino group and a carboxylic acid group substituent on the same carbon
atom, with the exception of proline, (has a secondary amino group)
Non-Standard Amino Acids
•Selenocysteine, 21st protein L-α amino acids
•Selenium atom replaces the sulfur of its elemental analog, cysteine
•Selenocysteine is not the product of a posttranslational modification, but is inserted directly into
a growing polypeptide during translation.
• Selenocysteine is charged on a special tRNA called tRNASec specific for UGA (STOP)codon
inserted into growing polypeptide during translation
Other Classification of Amino Acids
•Non-protein aa: Not naturally encoded by genetic code but found in free state as intermediates
of metabolic pathway for standard aa: Ornithine and citrulline are intermediates in urea
biosynthesis.
• Non α-aa: -NH: 2 group not attached to α-carbon atom but some other carbon
atom. Example. γ-aminobutyric acid (GABA) and β-alanine.
•Modified protein aa: Amino acids modified after they incorporated into protein.
Proline and lysine undergo hydroxylation to become hydroxyproline and
Hydroxylysine. Essential for formation of mature collagen
AA Classified on Basis of Nutritional Requirement
•Essential amino acids: Not synthesised in the body and must be supplied in diet
•Non-essential amino acids: Synthesized in body and there is no diet dependency for them
•Semi-essential amino acids: Not synthesised in the body in adequate amounts and requires
dietary supplementation.

AA Classified on Basis of metabolic classification


•Ketogenic amino acids: Only two aa are ketogenic, ex. Lysine and leucine. They catabolically
give intermediates convertible into acetyl-CoA or acetoacetyl-CoA
•Glucogenic amino acids: Those aa give rise to intermediates of glycolysis or Kreb‘s cycle
convertible by gluconeogenesis into glucose. Ex. Arg, His etc.
•Mixed amino acids: There are aa, carbon skeleton of which catabolized to produce the
glycolytic intermediates as well as acetyl-CoA derivatives. Ex. Phe, Try.
Amino-Acids Classification Based on Side Chain Groups
•Based on type of functional group (R group) present amino acids are classified as: Aliphatic,
aromatic, acidic, basic, acid amide, sulfur and cyclic amino acids.
•Based on characteristic of functional group amino acids are classified as: polarand non-polar
amino acids.
•Based on site of attachment of functional group. They are also classified as: alpha, beta,
gamma and delta amino acids

Amino Acids Classification based on hydrophobic and hydrophilic property


Structure of amino acids
Neutral, nonpolar side Chains

Neutral, polar side chains


Basic, polar side chains

Acidic, polar side chains

Function of Essential Amino acids


Non-polar amino acids:
1. Aromatic aa:
a) Phenylalanine: precursor for tyrosine, dopamine, nor-epinephrine, epinephrine and melanin.
•Genetic disorder phenylketonuria is the inability to metabolize phenylalanine because of a lack
of phenylalanine hydroxylase.
a) Tryptophan: precursor for neurotransmitter (serotonin), hormone (melatonin) and vitamin
niacin. Trp and Tyr residues anchoring membrane proteins within cell membrane.
•Fructose malabsorption causes improper absorption of Trp in intestine causes reduced level of
Trp in blood
2. Aliphatic amino acids:
a) Alanine: Alanine synthesized from pyruvate and branched chain aa. It plays
an imp. role in glucose-alanine cycle between tissues and liver.
•This cycle enables pyruvate and glutamate to be removed from muscle and
safely transported to liver.
•Alteration in alanine cycle increase the level of ALT (Alanine transferases) which
linked to the development of type II diabetes.
b) Valine: Essential for hematopoietic stem cell (HSC) self-renewal.
•In sickle-cell disease, a single glutamic acid in β-globin replaced with valine because valine is
hydrophobic, whereas glutamic acid is hydrophilic, this change makes the Hb prone to bnormal
aggregation.
c) Leucine: Primary metabolic end products of leucine metabolism are acetyl-CoA and
acetoacetate. It is also a imp ketogenic aa.
•Adipose and muscle tissue use leucine in the formation of sterols.
•MSUD caused by deficiency of branched chain α-keto acid dehydrogenase complex leading to
build-up branched chain aa and their toxic product ketoacids present in blood and urine.
c) Isoleucine: diverse physiological functions, such as assisting wound healing, detoxification of
nitrogenous wastes, stimulating immune function, and promoting secretion of several hormones.
3. Sulfur-containing aa:
a) Methionine: Substrate for other amino acids such as cysteine and taurine, versatile
compounds such as S-adenosyl methionine and antioxidant glutathione.
•Homocysteine can be used to regenerate methionine or to form cysteine.
•Improper conversion of methionine can lead to atherosclerosis due to accumulation of
homocysteine.
Polar uncharged aa:
1. Threonine: Its residue ssusceptible to numerous posttranslational modifications.
•The hydroxyl side-chain undergo O-linked glycosylation.
•Threonine residues undergo phosphorylation through the action of a threonine kinase. In its
phosphorylated form, it can be referred to as phosphothreonine. Its role in cell signal
transduction and neural activity.
Polar Charged amino-acids:
1. Positive charge/Basic aa:
a) Histidine: precursor for histamine, an amine produced in the body necessary for
inflammation.
•Histidine ammonia-lyase converts histidine into ammonia and urocanic acid. Deficiency in this
enzyme in rare metabolic disorder histidinemia.
b) Lysine: Lysine can also contribute to protein stability as its ε-amino group often participates
in hydrogen bonding, salt bridges and covalent interactions to form a Schiff base.
•A second major role of lysine is in epigenetic regulation by means of histone modification.
•It plays a key role in other biological processes including; structural proteins of connective
tissues, calcium homeostasis and fatty-acid metabolism.
•Due to a lack of lysine catabolism, the amino acid accumulates in plasma and patients develop
hyperlysinaemia
Notes
•Both α-amino acids and non-α-amino acids occur in nature, but proteins are
synthesized using only L-α-amino acids.
•The R groups of amino acids determine their unique biochemical functions.
•Amino acids are classified as basic, acidic, aromatic, aliphatic, or sulfurcontaining based on the
composition and properties of their R groups.
Protein Function
• Proteins perform crucial roles in all biological processes.
1. Catalytic function: Nearly all reactions in living organisms are catalyzed by proteins
functioning as enzymes. Without these catalysts, biological reactions would proceed much more
slowly.
2. Structural function: In animals structural materials other than inorganic components of the
skeleton are proteins, such as collagen (mechanical strength of
skin and bone) and keratin (hair, skin, fingernails).
3. Storage function: Some proteins provide a way to store small molecules or ions, e.g.,
ovalbumin (used by embryos developing in bird eggs), casein (a milk
protein) and gliadin (wheat seeds), and ferritin (a liver protein which complexes with iron ions).
4. Protective function: Antibodies are proteins that protect the body from disease by combining
with and destroying viruses, bacteria, and other foreign
substances. Another protective function is blood clotting, carried out by thrombin and fibrinogen.
5. Regulatory function: Body processes regulated by proteins include growth (growth hormone)
and thyroid functions (thyrotropin).
6. Nerve impulse transmission: Some proteins act as receptors for small molecules that
transmit impulses across the synapses that separate nerve cells (e.g.,
rhodopsin in vision).
7. Movement function: The proteins actin and myosin are important in muscle activity,
regulating the contraction of muscle fibers
8. Transport function: Some proteins bind small molecules or ions and transport them through
the body.
– Serum albumin is a blood protein that carries fatty acids between fat (adipose) tissue and other
organs.
– Hemoglobin carries oxygen from the lungs to other body tissues.
– Transferrin is a carrier of iron in blood plasma.
• A typical human cell contains 9000 different proteins; the human body contains about 100,000
different proteins

Biological Functions of Proteins


Protein Structure
• The structure of proteins is much more complex than that of simple organic molecules.
– Many protein molecules consist of a chain of amino acids twisted and folded into a complex
three-dimensional structure
– The complex 3D structures of proteins impart unique features to proteins that allow them to
function in diverse ways.
• There are four levels of organization in proteins structure: primary, secondary, tertiary, and
quaternary

Characteristics of Proteins

Stereochemistry of the Amino Acids


• Since the amino acids (except for glycine) contain four different groups connected to the -
carbon, they are chiral, and exist in two enantiomeric forms:
All living organisms appear to use only L – amino acids to assemble proteins and many
organisms are not genetically programmed to synthesize or utilize their D enantiomers.
Some bacteria produce enzymes that catalyze the interconversion of D and L enantiomers. The
newly formed D enantiomer is used to construct bacterial cell walls.

Acid-Base Properties
• Proteins take the form of zwitterions. They have characteristic isoelectric points, and can
behave as buffers in solutions.
• The tendency for large molecules to remain in solution or form stable colloidal dispersions
depends on the repulsive forces acting between molecules with like charges on their surfaces.
– When proteins are at a pH in which there is a net positive or negative charge, the like charges
cause the molecules to repel one another, and they remain dispersed.
– When the pH is near the isoelectric point, the net charge on the molecule is zero, and the
repulsion between proteins is small. This causes the protein molecules to clump and precipitate
from solution

Zwitterions
• Because amino acids contain both an acidic and a basic functional group, an internal acid-base
reaction occurs, forming an ion with both a positive and anegative charge called a zwitterions.
In solution, the structure of an amino acid can change with the pH of the solution

 Lowering the pH of the solution causes the zwitterion to pick up a proton:

Increasing the pH of the solution causes the zwitterion to lose a proton:

Since the pH of the solution affects the charge on the amino acid, at some pH, the amino acid
will form a zwitterion. This is called the isoelectric point.
• Each amino acid (and protein) has a characteristic isoelectric point: those with neutral R groups
are near a pH of 6, those with basic R groups have higher values, and those with acidic R groups
have lower values.
• Because amino acids can react with both H3O+ and OH-, solutions of amino acids and proteins
can act as buffers. (E.g., blood proteins help to regulate the pH of blood.
Reaction of Amino acids:
Amino acids can undergo any of the reactions characteristic of the functional groups in the
structure.
• Cysteine is the only amino acid that contains a sulfhydryl (thiol, R—SH) group. Thiols are
easily oxidized to form disulfide bonds (R—S—S—R).
This allows cysteine to dimerize to form cystine:

Peptide Formation
Peptide Bond
The crucial feature of amino acids that allows them to polymerize to form peptides and proteins
is the existence of their two identifying chemical groups: the amino (-NH3+) and carboxyl (-
COO-) groups, The amino and carboxyl groups of amino acids can react in a head-to-tail fashion,
eliminating a water molecule and forming a covalent amide linkage, which, in the case of
peptides and proteins, is typically referred to as a peptide bond. The equilibrium for this
reaction in aqueous solution favors peptide bond hydrolysis. For this reason, biological systems
as well as peptide chemists in the laboratory must carry out peptide bond formation in an indirect
manner or with energy input.
Iteration of the reaction shown in Figure 2 produces polypeptides and proteins. The remarkable
properties of proteins, all depend in one way or another on the unique properties and chemical
diversity of the 20 common amino acids found in proteins.

 Amino acids are linked together by ‗amide groups’ called peptide bonds.
 During protein synthesis, the carboxyl group of amino acid at the end of the growing
polypeptide chain reacts with the amino group of an incoming amino acid, releasing a
molecule of water. The resulting bond between the amino acids is a peptide bond.

Proteins come in many different shapes and sizes. Some are globular (roughly spherical) in
shape, whereas others form long, thin fibers. For example, the hemoglobin protein that carries
oxygen in the blood is a globular protein, while collagen, found in our skin, is a fibrous protein.
A protein‘s shape is critical to its function, and, as we‘ll see in the next article, many different
types of chemical bonds may be important in maintaining this shape. Changes in temperature and
pH, as well as the presence of certain chemicals, may disrupt a protein‘s shape and cause it to
lose functionality, a process known as denaturation.

• Amides can be thought of as forming from the reaction of an amine and a carboxylic acid:

• In the same way, two amino acids can combine to form a dipeptide, held together by a peptide
bond:

The two amino acids can connect the other way as well, forming a structural isomer of the
dipeptide, with a unique set of physical properties:
• A third amino acid can join the chain to form a tripeptide:

A fourth amino acid would form a tetrapeptide, a fifth would form a pentapeptide, and so on.
• Short chains are referred to as peptides, chains of up to about 50 amino acids are polypeptides,
and chains of more than 50 amino acids are proteins.
(The terms protein and polypeptide are often used interchangeably.)
• Amino acids in peptide chains are called amino acid residues.
– The residue with a free amino group is called the N-terminal residue, and is written on the left
end of the chain.
– The residue with a free carboxylate group is called the C-terminal residue, and is written on
the right end of the chain
Peptides are named by starting at the N-terminal end and listing the amino acid residues from left
to right.
• Large amino acid chains are unwieldy to draw in their complete forms, so they are usually
represented by their three-letter abbreviations, separated by
dashes:
– Gly-Ala (Gly = N-terminal, Ala = C-terminal)
– Ala-Gly (Ala = N-terminal, Gly = C-terminal)
• The tripeptide alanylglycylvaline can be written as Ala-Gly-Val. (There are five other
arrangements of these amino acids that are possible.)
• Insulin has 51 amino acids, with 1.551066 different possible arrangements, but the body
produces only one.
Nonapeptide proteins

Vasopressin and Oxytocin


• More than 200 peptides have been identified as being essential to the body‘s proper
functioning.
• Vasopressin and oxytocin are nonapeptide hormones secreted by the pituitary gland. Six of the
amino acid residues are held in a loop by disulfide bridges formed by the oxidation of two
cysteine
residues. Even though the molecules are very similar, their biological functions are quite
different:
– Vassopressin is known as antidiuretic hormone (ADH) because it reduces the amount of urine
formed, which causes the body to conserve water. It also raises blood pressure.
– Oxytocin causes the smooth muscles of the uterus to contract, and is administered to induce
labor. It also stimulates the smooth muscles of mammary glands to stimulate milk ejection.

Adrenocorticotropic hormone
• Adrenocorticotropic hormone (ACTH) is a 39-residue peptide produced in the pituitary gland.
It regulates the production of steroid hormones in the cortex of the adrenal gland.
Size of Proteins
• Proteins are very large polymers of amino acids with molecular weights that vary from 6000
amu to several million amu.
– Glucose (C6H12O6) = 180 amu
– Hemoglobin (C2952H4664O832N812S8Fe4) = 65,000 am

Proteins are too large to pass through cell membranes, and are contained within the cells where
they were formed unless the cell is damaged by disease or trauma.
– Persistent large amounts of protein in the urine are indicative of damaged kidney cells.
– Heart attacks can also be confirmed by the presence of certain proteins in the blood that are
normally confined to cells in heart tissue.

Levels of Protein Structure


For large macromolecules such as proteins, the tasks of describing and understanding structure
are approached at several levels of complexity, arranged in a kind of conceptual hierarchy. Four
levels of protein structure are commonly defined A description of all covalent bonds (mainly
peptide bonds and disulfide bonds) linking amino acid residues in a polypeptide chain is its
primary structure. The most important element of primary structure is the sequence of amino
acid residues. Secondary structure refers to particularly stable arrangements of amino acid
residues giving rise to recurring structural patterns. Tertiary structure describes all aspects of
the three-dimensional folding of a polypeptide. When a protein has two or more polypeptide
subunits, their arrangement in space is referred to as quaternary structure.
Figure: Visualizing Protein Structure

Primary Structure of Proteins


• The primary structure of a protein is the linear sequence of the side chains that are connected
to the protein backbone:

Each protein has a unique sequence of amino acid residues that cause it to fold into a distinctive
shape that allows the protein to function properly.
• Primary structure of human insulin:

Secondary Structure —
The a Helix
• Hydrogen bonding causes protein chains to fold and align to produce orderly patterns called
secondary structures.
The a-helix is held in this shape by hydrogen bonding interactions between amide groups, with
the side chains extending outward from the coil.
• The amount of a-helix coiling in proteins is highly variable
In a-keratin (hair, pictured below), myosin (muscles), epidermin (skin), and fibrin (blood clots),
two or more helices coil together (supracoiling) to form cables. These cables make up bundles
of fibers that strengthen tissues in which they are found:

The b-Pleated Sheet


• Another secondary structure is the b-pleated sheet, in which several protein chains lie side by
side, held by hydrogen bonds between adjacent chains:
The b-pleated sheet structure is less common than the a-helix; it is found extensively only in the
protein of silk.
• The figure below shows both types of secondary structures in a single protein.

Tertiary Structure of Proteins


• The tertiary structure of a protein refers to the bending and folding of the protein into a
specific three-dimensional shape.
• These structures result from four types of interactions between the R side chains of the amino
acids residues:
1. Disulfide bridges can form between two cysteine residues that are close to each other in the
same chain, or between cysteine residues in different chains. These bridges hold the protein
chain in a loop or some other 3D shape.
2. Salt bridges are attractions between ions that result from the interactions of the ionized side
chains of acidic amino acids (—COO-) and the side chains of
basic amino acids (—NH3+).
3. Hydrogen bonds can form between a variety of side chains, especially those that contain:

Hydrogen bonding also influences the secondary structure, but here the hydrogen bonding is
between R groups, while in secondary structures it is between the C=O and NH portions of the
backbone.

4. Hydrophobic interactions result from the attraction of nonpolar groups, or when they are
forced together by their mutual repulsion of the aqueous solvent.
These interactions are particularly important between the benzene rings in phenylalanine or
tryptophan. This type of interaction is relatively
weak, but since it acts over large surface areas, the net effect is a strong interaction.
4. cont. The compact structure of globular proteins in aqueous solution, in which the nonpolar
groups are pointed inward, away from the water molecules.
Quaternary Structure of Proteins
• When two or more polypeptide chains are held together by disulfide bridges, salt bridges,
hydrogen bond, or hydrophobic interactions, forming a larger protein complex.
• Each of the polypeptide subunits has its own primary, secondary, and tertiary structure.
• The arrangement of the subunits to form a larger protein is the quaternary structure of the
protein.
Hemoglobin
• Hemoglobin is made of four subunits: two identical alpha chains containing 141 AA‘s and two
identical beta chains containing 146 AA‘s. Each subunit contains a heme group located in
crevices near the exterior of the molecule

Protein Hydrolysis and Denaturation


Protein Hydrolysis
• Amides can be hydrolyzed under acidic or basic conditions.
• The peptide bonds in proteins can be broken down under acidic or basic conditions into smaller
peptides, or all the way to amino acids, depending on the hydrolysis time, temperature, and pH

– The digestion of proteins involves hydrolysis reactions catalyzed by digestive enzymes.


– Cellular proteins are constantly being broken down as the body resynthesizes molecules and
tissues that it needs

Denaturation
• Proteins are maintained in their native state (their natural 3D conformation) by stable
secondary and tertiary structures, and by aggregation of subunits into quaternary structures.
• Denaturation is caused when the folded native structures break down because of extreme
temps. Or pH values, which disrupt the stabilizing structures.
The structure becomes random and disorganized.

Denaturation
• Most proteins are biologically active only over a temperature range of 0ºC to 40ºC.
• Heat is often used to kill microorganisms and deactivate their toxins. The protein toxin from
Clostridium botulinum is inactivated by being heated to 100ºC for a few minutes; heating also
deactivates the toxins that cause diphtheria and tetanus.
• Heat denaturation is used to prepare vaccines against some diseases. The denatured toxin can
no longer cause the disease, but it can stimulate the body to
produce substances that induce immunity.

Denaturation
• Proteins can also be denatured by heavy-metal ions such as Hg2+, Ag+, and Pb2+ hat interact
with —SH and carboxylate groups.
– Organic materials containing Hg (mercurochrome and merthiolate) were common topical
antiseptics.
– Heavy-metal poisoning is often treated with large doses of raw egg white and milk; the
proteins in the egg and milk bind to the metal ions, forming a precipitate, which is either vomited
out or pumped out
Reference Books
1) Harper‘s Illustrated Biochemistry-30th edition
2) Textbook of Biochemistry with Clinical Correlations. 4th edition. Thomas M. Devlin.
3) Biochemistry. 4th edition. Donald Voet and Judith G. Voet.
4) Biochemistry 7th edition by Jeremy M. Berg, John L. Tymoczko and Lubert Stryer
5) Lehninger Principles of Biochemistry
6) Netter's essential biochemistry 1st Ed
7) https://en.wikipedia.org/wiki/aminoacids

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