PROTEINS

CHON
PROTEINS
- the most important of all
biological compounds Classification based on Functions:

● STRUCTURAL
- present in every cell of humans,
animals, plant tissues, tissue fluids ● CATALYTIC /ENZYMIC
and in microorganisms. ● CONTRACTILE
● TRANSPORT/CARRIER
- derived from the Greek proteios,
meaning “of first importance”.
PROTEINS Classification based on Functions:

- the most important of all ● STRUCTURAL

biological compounds ● CATALYTIC /ENZYMIC
● CONTRACTILE
- present in every cell of humans, ● TRANSPORT/CARRIER
animals, plant tissues, tissue ● DEFENSE
fluids and in microorganisms. ● NUTRIENT AND STORAGE
● REGULATORY
- derived from the Greek proteios,
meaning “of first importance”.
*PATHOGENIC

*TOXIC
 PRIONS
spongiform encephalopathy
Creutzfeldt-Jakob disease (CJD) is a rapidly
progressive, invariably fatal neurodegenerative
disorder believed to be caused by an abnormal
isoform of a cellular glycoprotein known as the prion
protein.
Mad cow disease, also called Creutzfeldt-Jakob
Disease (CJD), is a fatal disease that slowly destroys
the brain and spinal cord in cattle. People cannot get
mad cow disease. However, in rare cases they can get
a human form of mad cow disease called variant
Creutzfeldt-Jakob disease (vCJD), which is also fatal.

Protein misfolding is believed to be the primary

cause of Alzheimer's disease, Parkinson's
disease, Huntington's disease, Creutzfeldt-Jakob
disease, cystic fibrosis, Gaucher's disease and
many other degenerative and neurodegenerative
disorders.
1. Simple Proteins
- On acid hydrolysis, yield only
amino acids

2. Conjugated Proteins
- On hydrolysis -
acid/basic/enzymatic, yield
amino acids and non-amino
acid group (aka prosthetic
group)
- further classified into
subclasses based on
prosthetic groups
Classification Acc. to COMPOSITION
3. Derived Proteins
- Formed from simple and conjugated b.) Secondary derived proteins
proteins (natural proteins)
- Formed from partial hydrolysis
of proteins
a.) Primary derived proteins
- Denatured proteins
- formed from natural proteins by the - Examples: Proteases, peptone,
action of heat or alcohol etc. The gelatin, and peptides.
peptide bonds are not hydrolysed
- Example: Coagulated proteins like
cooked-egg albumin
Classification based on STRUCTURE
2.) Fibrous proteins
1.) Globular proteins
- Aka SPHEROPROTEINS - Aka
- Elliptical or spherical shape SCLEROPROTEINS
- Soluble with water, acid and base; - Strand-like structures;
forms a colloidal solution with rods and wires
water - Soluble in strong
acids and alkalis
- E.g. enzymes, antibodies and
some hormones (insulin)
 AMINO ACIDS
- Building blocks of proteins
- organic compound containing an amino group
and a carboxyl group
-
- The 20 amino acids commonly found in
proteins are called alpha amino acids -the
amino group is linked to the carbon atom next
to the —COOH carbon.
AMINO ACIDS All of the 20 fit the formula except PROLINE: R is bonded to H
CLASSIFICATION OF AMINO ACIDS BASED ON THE SIDE CHAINS (R)

1. Nonpolar
- ALKYL/ALIPHATIC
- AROMATIC
2. Polar
- NEUTRAL
- ACIDIC
- BASIC
AMINO ACIDS
An amino acid has -COOH and -NH2 groups in the
ZWITTERIONS
same molecule. Therefore, the -COOH donates a
- Compounds that have a positive charge on proton to the -NH2 so that an amino acid actually
has the structure:
one atom and a negative charge on
another; has an overall neutral charge

Carboxylic acids, RCOOH, cannot exist in the

presence of a moderately weak base (such as
NH3). They donate a proton to become
carboxylate ions, RCOO. Likewise, amines,
RNH2, cannot exist as such in the presence of a
moderately weak acid. They gain a proton to
become substituted ammonium ions, RNH3. Isoelectric point (pI)
- A pH at which a sample of amino acids or
protein has an equal number of positive and
negative charges
AMINO ACIDS Acid solution

An amino acid has -COOH and -NH2 groups in

the same molecule. Therefore, the -COOH donates
a proton to the -NH2 so that an amino acid
actually has the structure:
- H3O donates a proton to the -COO2
- happens to all amino acids if the pH is
sufficiently lowered
- Generally CATIONS

Alkaline solution

Isoelectric point (pI) - Addition of -OH2 causes the -NH3 to donate its
- A pH at which a sample of amino acids or proton to -OH2
- This happens to all amino acids if the pH is
protein has an equal number of positive and
sufficiently raised
negative charges (Zwitterions) - Generally ANIONS
ESSENTIAL AMINO ACIDS
1.) Arginine (Arg)

- generation of urea-necessary for the removal of toxic ammonia from the

body

- synthesis of creatine, which degrades to creatinine-a waste product that is

cleared from the body by the kidney
ESSENTIAL AMINO ACIDS
2.) Histidine (His)

-
- direct precursor of histamine
- source of carbon atoms in the synthesis of purines
- stimulates the secretion of the digestive enzyme gastrin and acts as a
catalytic site in certain enzymes
- helps to protect the body from heavy metal toxicity.
ESSENTIAL AMINO ACIDS
3.) Lysine

- production of antibodies and lowers triglyceride levels.

- maintain a proper nitrogen balance in adults.

- helps in the absorption and conservation of calcium and plays an important

role in the formation of collagen
ESSENTIAL AMINO ACIDS
4.) Methionine (Met)

- helps to initiate translation of messenger RNA by being the first amino acid
incorporated into the N-terminal position of all proteins.
- prevents brittle hair
- reacts with adenosine triphosphate to contribute to the synthesis of many
important substances, including epinephrine and choline
ESSENTIAL AMINO ACIDS
5.) Threonine (Thr)

- alcohol-containing amino acid that is an important component in the

formation of protein, collagen, elastin (a connective tissue protein), and
tooth enamel
- important in the production of neurotransmitters and health of the
nervous system
- helps maintain proper protein balance in the body and it aids liver
function, metabolism, and assimilation
ESSENTIAL AMINO ACIDS
6.) Tryptophan (Trp)

- formed from proteins during digestion by the action of proteolytic enzymes

- A precursor for serotonin and melatonin, a neurohormone and powerful
antioxidant.
- a natural relaxant
- used in the treatment of migraine headaches, aids in weight control by
reducing appetite, and helps control hyperactivity in children.
ESSENTIAL AMINO ACIDS
7.) Isoleucine (Ile)

- Branched amino acid

- needed for hemoglobin formation

- it helps to regulate blood glucose levels and maintain energy levels

ESSENTIAL AMINO ACIDS
8.) Leucine (Leu)

- Branched amino acid

- second most common amino acid found in protein beside glycine
- lowers blood glucose levels.
- necessary for the optimal growth of infants and for nitrogen balance in
adults
ESSENTIAL AMINO ACIDS
9.) Valine (Val)

- Branched amino acid used by muscle tissue as an energy source.

- used in treatments for muscle, mental, and emotional problems; insomnia;

anxiety; and liver and gallbladder disease.
ESSENTIAL AMINO ACIDS
10.) Phenylalanine (Phe)

- used by the brain to produce norepinephrine, a neurotransmitter

- in large quantities, interferes with the production of serotonin
- composition of aspartame, a common sweetener used in prepared foods as a
sugar replacement.
NON-ESSENTIAL AMINO ACIDS
1. ) Alanine (Ala)

- a product of the breakdown of DNA or

the dipeptides anserine and carnosine, and the conversion of pyruvate, a
pivotal compound in carbohydrate metabolism
- plays a major role in the transfer of nitrogen from peripheral tissue to the liver,
helps in reducing the buildup of toxic substances that are released into muscle
cells when muscle protein is broken down quickly to meet energy needs, and
strengthens the immune system through production of antibodies.
NON-ESSENTIAL AMINO ACIDS
2.) Cysteine (Cys)

- named after cystine, its oxidized dimer.

- potentially toxic and is catabolized in the gastrointestinal tract and blood.
- In opposition, cysteine is absorbed during digestion as cystine, which is more stable in
the gastrointestinal tract. It is cystine that travels to cells, where it is reduced to two
cysteine molecules upon cell entry.
- One of its largest applications is in the production of flavors.
NON-ESSENTIAL AMINO ACIDS
3.) Asparagine (Asn)

- isolated in 1806 from asparagus juice, becoming the first amino acid to be
isolated.
- frequently the most abundant of the amino acids involved in the transport of
nitrogen
- The main function of asparagine is converting one amino acid into another via
amination- process by which an amine group is introduced into an organic
molecule, and transamination- the reaction when an amino acid is transferred to
an ⍺-ketoacid. Asparagine is required by the nervous system and plays an
important role in the synthesis of ammonia.
NON-ESSENTIAL AMINO ACIDS
4.) Aspartic Acid (Asp)

- alanine with one of the ꞵ hydrogens replaced by a carboxylic acid group

- vital role in metabolism during construction of other amino acids and
metabolites in the citric acid cycle
- also a metabolite in the urea cycle and participates in gluconeogenesis
NON-ESSENTIAL AMINO ACIDS
5.) Glutamic Acid (Glu)

- synthesized from a number of amino acids, and when an amino group is added to
glutamic
acid, it forms the important amino acid glutamine.
- linked to epileptic seizures, is a neurotransmitter, is important in the metabolism of
sugars and fats, and aids transporting potassium into the spinal fluid.
- Umami taste
NON-ESSENTIAL AMINO ACIDS
6.) Glutamine (Gln)

- most abundant amino acid in the body

- >61% of skeletal muscle tissue is glutamine
- converted to glucose when more glucose is required for energy and aids in immune
function.
- the basis of the building blocks for the synthesis of RNA and DNA- nitrogen donor
for purine and pyrimidine synthesis
- !Glutamine transports ammonia, the toxic metabolic byproduct of protein
breakdown, to the liver, where it is converted into less toxic urea and then excreted
by the kidneys!
NON-ESSENTIAL AMINO ACIDS

7.) Glycine (Gly)

- simplest amino acid synthesized in the

body and is the only amino acid that is not optically active
- The liver uses glycine to help in the detoxification of compounds and to help in
the synthesis of bile acids
- inhibitory neurotransmitter in the central
nervous system (CNS)
NON-ESSENTIAL AMINO ACIDS
8.) Proline (Pro)

- precursor of hydroxyproline, which is manufactured into collagen, tendons,

ligaments, and heart muscle by the body
- plays important roles in molecular recognition, and is an important
component in certain medical wound dressings that use collagen to stimulate
wound healing
NON-ESSENTIAL AMINO ACIDS
9.) Serine (Ser)

- the second amino acid that is also an alcohol because of its methyl side chain,
which contains a hydroxy group
- proper metabolism of fats and fatty acids and plays an important role in the
body’s synthetic pathways for pyrimidines, purines (making it
important for DNA and RNA function), creatine, and porphyrins.
- component of the protective myelin sheaths surrounding nerve fibers, and
aids in the production of immunoglobulins and antibodies for the maintenance
of a healthy immune system.
NON-ESSENTIAL AMINO ACIDS
10.) Tyrosine (Tyr)

- metabolically synthesized from the important

amino acid phenylalanine to become the para-hydroxy derivative of phenylalanine
- Synthesis of L-DOPA (Levodopa)- precursor of CATECHOLAMINES
- Melanin production- After the formation of DOPA from tyrosine, the further conversion
of DOPA to DOPAquinone follows. Then, a number of intermediates are formed
ending in indolequinone that polymerizes to form melanin. The more common
product is eumelanin (brown) but in the presence of cysteine, pheomelanin can be
formed (red to yellow).
 TWO NEW AMINO ACIDS
.) Selenocysteine (Sec) 2.) Pyrrolysine (Pyl)
- recognized as the 21st amino acid
- selenium analogue of cysteine
- it is not coded for directly in the genetic code;
encoded by a UGA codon, which is normally a stop
codon
- It has been discovered that HIV-1 encodes a
functional selenoprotein, and patients with HIV
infection have been shown to have a
lower-than-average blood plasma selenium level.
- 22nd naturally occurring genetically encoded
amino acid used by some archaea and
single-celled microorganisms in enzymes that
are part of their methane-producing
metabolism.
- encoded by the UAG codon, normally a stop
codon, possibly modified by the presence of a
specific downstream sequence forcing the
incorporation of pyrolysine instead of
terminating translation