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Functions and Properties of Proteins, Lecture notes of Biochemistry

University of Perpetual Help (UPH)Biochemistry

A comprehensive overview of proteins, a class of biomolecules crucial for biological processes. It covers their sources, building blocks (amino acids), types, functions, deficiencies, and excess conditions. The document also discusses protein structures and classification, as well as factors causing denaturation. This information is valuable for students and researchers in biochemistry, molecular biology, and related fields.

Typology: Lecture notes

2022/2023

Available from 08/26/2024

zyrene-joy-motita 🇵🇭

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1 | P r o t e i n s

PROTEINS

 FUNCTIONS OF PROTEINS

 Building of new cells

 Maintenance of existing cells

 Replacement of old cells

 Source of energy

 Regulation of metabolic process (hormone)

 Catalysis of biochemical reactions (enzymes)

 Transportation of oxygen (hemoglobin)

 Body’s defense against infection (antibodies)

 Transmission of impulses (nerves)

 Transmission of hereditary characteristics (nucleoproteins)

 Muscular activity (contraction)

 SOURCES OF PROTEINS

 Plants synthesized proteins from inorganic substances present i n air and in the soil

 Animals cannot synthesized proteins from such materials

 Animals must obtain proteins from plants or from other animals

 WHAT BODY PARTS PROTEIN ARE PRESENT?

 Skin

 Hair

 Nails

 Connecting tissue

 Supporting tissue

AMINO ACIDS

- The building block for proteins

 Protein is derived from the Greek word proteios, which means “of first importance”

 Protein is a polymer in which the monomer units are amino acids

 Hydrolysis of proteins yields amino acids

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PROTEINS

 FUNCTIONS OF PROTEINS

 Building of new cells  Maintenance of existing cells  Replacement of old cells  Source of energy  Regulation of metabolic process (hormone)  Catalysis of biochemical reactions (enzymes)  Transportation of oxygen (hemoglobin)  Body’s defense against infection (antibodies)  Transmission of impulses (nerves)  Transmission of hereditary characteristics (nucleoproteins)  Muscular activity (contraction)  SOURCES OF PROTEINS  Plants synthesized proteins from inorganic substances present in air and in the soil  Animals cannot synthesized proteins from such materials  Animals must obtain proteins from plants or from other animals  WHAT BODY PARTS PROTEIN ARE PRESENT?  Skin  Hair  Nails  Connecting tissue  Supporting tissue AMINO ACIDS

The building block for proteins  Protein is derived from the Greek word proteios, which means “of first importance”  Protein is a polymer in which the monomer units are amino acids  Hydrolysis of proteins yields amino acids

 NON-POLAR AMINO ACIDS

 Alanine

Non-Essential | Proteogenic | Glycogenic | Non-Polar | Hydrophobic | Aliphatic Main Function
Important source of energy for muscle
Primary amino acid in sugar metabolism
Boosts immune system by producing antibodies
Major part of connective tissue Deficiencies
HYPOGLYCEMIA
MUSCLE BREAKDOWN
FATIGUE
VIRAL INFECTIONS
ELEVATED INSULIN AND GLUCAGON LEVELS EXCESS (SEEN IN)
Low insulin and glucagon levels
Diabetes mellitus
Kwashiorkor (starvation)  Isoleucine
Essential | Proteogenic | Glycogenic and Ketogenic Non-Polar | Hydrophobic | Aliphatic Main Functions
One of 3 major Branched-Chain Amino Acids (BCAA)
Involved in muscle strength, endurance, and muscle stamina
Muscle tissue use Isoleucine as an energy source
Required in the formation of hemoglobin Deficiency
Obesity
Hyperinsulinemia
Panic Disoorder
Chronic Fatigue Syndrome
Acute Hunger
Kwashiorkor EXCESS (SEEN IN)
Diabetic Mellitus with Ketotic Hypoglycemia  Leucine
Essential | Proteogenic | Ketogenic | Non-Polar | Hydrophobic | Aliphatic Main Functions
One of the 3 (BCAA) together with Isoleucine and Valine
Potent stimulator of insulin
Helps with bone healing

 Proline

NON-ESSENTIAL | PROTEOGENIC | GLYCOGENIC | NON-POLAR | HYDROPHOBIC | ALIPHATIC Main Function
Component of cartilage, and hence health of joints, tendons and ligaments
Involved in keeping heart muscle strong
Main precursor to Proline is Glutamine
Works in conjunction with Vitamin C in keeping skin and joints healthy EXCESS (SEEN IN)
CHRONIC LIVER DISEASE
SEPSIS (INFECTION OF THE BLOOD)
ACUTE ALCOHOL INTAKE  Tryptophan
ESSENTIAL | PROTEOGENIC | GLYCOGENIC AND KETOGENIC | NON-POLAR | HYDROPHOBIC | AROMATIC Main Function
Exerts calming effect (serotonin)
Effective sleep aid, due to conversion to serotonin
Reduces anxiety
Treatment for migraine headaches
Stimulate GH
Lowers risk of arterial spasms
The only plasma amino acid that is bound to protein Deficiency
DEPRESSION
INSOMNIA
CHRONIC FATIGUE SYNDROME
ALS
FDA BAN OF TRYPTOPHAN EXCESS (SEEN IN)
Increased intake of salicylates (aspirin)
Increased blood levels of free fatty acids
Sleep deprivation
Niacin intake  Valine
ESSENTIAL | PROTEOGENIC | GLYCOGENIC | NON-POLAR | HYDROPHOBIC | ALIPHATIC Main Functions
Actively absorbed and used directly by muscle as an energy source
Any acute physical stress (including surgery, sepsis, fever, trauma, starvation) requires higher amount of Valine, Leucine and Isoleucine that any of the other amino acids
During period of Valine deficiency all of the other amino acidsand proteins are less well absorbed by the GI tract

Deficiency

KWARSHIORKOR
HUNGER
OBESITY
NEUROLOGICAL DEFICIT
ELEVATED INSULIN LEVELS EXCESS (SEEN IN)
Ketotic Hypoglycemia
Visual and tactile hallucinations  POLAR AMINO ACIDS  Lysine
ESSENTIAL | PROTEOGENIC | GLYCOGENIC AND KETOGENIC | BASIC SIDE CHAINS Main Functions
Inhibits viral growth : used in treatment of; Herpes Simplex, viruses associated w/ CFS
L-Carnitine is formed from LYSINE and VITAMIN C
Helps form collagen , the connective tissue present in bones, ligaments, tendons, and joints
Assists in the absorption of calcium
Involved I hormone production
Lowers serum triglyceride levels Deficiency
HERPES
EPSTEIN-BARR VIRUS
CHRONIC FATIGUE SYNDROME
AIDS
ANEMIA
HAIR LOSS
WEIGHT LOSS
IRRITABILITY EXCESS (SEEN IN)
Excess of ammonia in the blood  Serine
NON-ESSENTIAL | PROTEOGENIC | GLYCOGENIC | IN-CHARGED | HYDROPHILIC | HYDROXYLIC Main Functions
One of the 3 most important glycogenic amino acids , (alanine and glycine)
Boosts immune system by assisting in production of antibodies and immunoglobulins
Required for growth and maintenance of muscle

- DRUG ADDICTION AND DEPENDENCY

EXCESS (SEEN IN)

Hyperthyroidism
Chronic liver disease, Cirrhosis Essential Amino Acids and the RDA in mg/kg body weight Adult Infant Isoleucine 28 70 Leucine 42 161 Lysine 44 103 Methionine 22 58 Phenylalanine 22 135 Threonine 28 87 Tryptophan 33 93 Valine 35 93 Histidine 28
must be obtained from the diet.
are ten amino acids not synthesized by the body.
are in meat and diary products.
are missing (one or more) in grains and vegetables.  PRIMARY STRUCTURES OF;  PROTEINS
The primary structure of a protein is
the particular sequence of amino acids.
the backbone of a peptide chain or protein.

 INSULIN

was the first protein to have its primary structure determined.
has a primary structure of two polypeptide chains linked by disulfide bonds.
has a chain A with 21 amino acids and a chain B with 30 amino acids.  SECONDARY STRUCTURES OF;  ALPHA – HELIX
a three-dimensional spatial arrangement of amino acids in a polypeptide chain.
held by H bonds between the H of – N-H group and the O of C=O of the fourth amino acid down the chain.
a corkscrew shape that looks like a coiled “telephone cord”.  BETA PLEATED SHEET
consists of polypeptide chains arranged side by side.
has hydrogen bonds between chains.
has R groups above and below the sheet.
is typical of fibrous proteins such as silk.  TRIPPLE HELIX
three polypeptide chains woven together.
typical of collagen, connective tissue, skin, tendons, and cartilage.  TERTIATY STRUCTURE OF A PROTEIN
is the overall three-dimensional shape.
is determined by attractions and repulsions between the side chains of the amino acids in a peptide chain.  GLOBULAR PROTEINS
have compact, spherical shapes.
carry out synthesis, transport, and metabolism in the cells.
such as myoglobin store and transport oxygen in muscle.  QUARTERNARY STRUCTURE
is the combination of two or more protein units.
of hemoglobin consists of four polypeptide chains as subunits.
is stabilized by the same interactions found in tertiary structures.  FIBROUS PROTEINS
consist of long, fiber-like shapes.
such as alpha keratins make up hair, wool, skin, and nails.
such as feathers contain beta keratins with large amounts of beta-pleated sheet structures.

Albuminoids Insoluble in all neutral solvents and in dilute acid and alkali no Keratin; nails; feathers; collagen Histones Soluble in salt solutions; insoluble in a very dilute NH 4 OH no Nucleohistone in thymus gland; globin in hemoglobin  CLASSIFICATION ACCORDING TO COMPOSITION Type Non-protein portion of the combination Examples Nucleoproteins Nucleic acid Chromosomes Glycoproteins Carbohydrates Mucin in saliva Phosphoproteins Phosphate Casein in milk Chromoproteins Chromophore group Hemoglobin, hemocyanin, flavoproteins, cytochrome Lipoproteins Lipids Fibrin in blood Metalloproteins Metals Ceruloplasmin (Cu) and siderophilin (Fe) in the blood plasma  GLYCOPROTEIN

Proteins containing carbohydrates
Molar mass from 15,000 to more than 1 million
Carbohydrates present include: hexoses, mannose, and galactose
Glucose is not found in glycoprotein, except for collagen
Present in animals, plants, bacteria, viruses, and fungi
Glycophorin is a glycoprotein found in the membrane of human erythrocytes
Heparin is also a glycoprotein  FUNCTIONS OF GLYCOPROTEIN IN MEMBRANES
As structural protein (collagen)
As lubricants (mucin and mucous secretions)
As transportation molecules for vitamins, lipids, minerals, and trace elements

As immunoglobulins such as interferon
As hormones such as thyrotropin (TSH)
As enzymes such as hydrolases and nucleases
As hormone receptor
For the specification of human blood types  LIPOPROTEIN
Proteins containing lipids
Chylomicrons are produced in the intestinal mucosa and are used to transport dietary lipids into the blood plasma via thoracic lymph duct
Chylomicrons are responsible for the creamed-tomato-soup appearance of blood following a meal containing fats
VLDL transport triglycerides synthesized by the liver to the other parts of the body
LDL provides cholesterol for cellular needs
HDL are involved in the catabolism of other lipoproteins; may also remove excess cholesterol form peripheral tissue
Women have higher HDL than men
Aerobic exercise increases HDL levels  PROPERTIES OF PROTEIN
Colloidal nature
Denaturation – refers to the unfolding and rearrangement of the secondary and tertiary structures of a protein without breaking the peptide bonds  Reagents or Conditions that Causes Denaturation
ALCOHOL
Alcohol coagulates (precipitate) all types of protein except prolamines
Alcohol (70%) is used as a disinfectant because of its ability to coagulate the protein present in bacteria
This process is not reversible
SALTS OF HEAVY METALS
Heavy metal salts such as mercuric chloride (bichloride of mercury) or silver nitrate (lunar causric) precipitate protein
Very poisonous if taken internally because they coagulate and destroy protein present in the body
Egg white can be an antidote when these heavy metals are taken internally
HEAT
Gentle heating causes reversible denaturation of protein
Vigorous heating denatures protein irreversibly
ALKALOIDAL REAGENTS
Tannic and picric acid form insoluble compounds with proteins
Tannic acid can be used in the treatment of burns
Wet tea bag contain tannic acid
RADIATION
Ultraviolet or x-ray can cause protein to coagulate
Denatures irreversibly
pH
Proteins are coagulated by strong acids
Casein is precipitated from milk as a curd when comes into contact with HCl in the stomach
Heller’s ring test is used to detect the presence of albumin in urine
OXIDIZING AND REDUCING AGENTS
Oxidizing agents such as bleach and nitric acid

Functions and Properties of Proteins, Lecture notes of Biochemistry

Related documents

Partial preview of the text

Download Functions and Properties of Proteins and more Lecture notes Biochemistry in PDF only on Docsity!

PROTEINS

 FUNCTIONS OF PROTEINS

 NON-POLAR AMINO ACIDS

- DRUG ADDICTION AND DEPENDENCY

EXCESS (SEEN IN)

 INSULIN