-A-

Acetyl Coenzyme A (or Acetyl-CoA)

- An important molecule in metabolism, used in many biochemical reactions. Its main function is to
convey the carbon atoms within the acetyl group to the citric acid cycle (Krebs cycle) to be oxidized
for energy production.
- A molecule produced in the mitochondria upon the oxidation of pyruvate and the reduction of
nicotinamide adenine dinucleotide (NAD+) to be used in the Krebs Cycle. Acetyl-CoA can also be
formed via the degradation of fatty acids.

Activation Energy
- The amount of energy required to bring the substrate to a transitional state.

Active Transport
- The process whereby ions are forced up their concentration gradient across a membrane.

Albumins
- From the Latin word albumen means (egg) white or dried egg white.
- Holoproteins and are a family of globular proteins that is widely distributed in nature, mostly seen in
seeds.
- They are soluble in water and dilute solutions of acids, bases and salts.
o Example: Leucosine, legumeline, serum albumin.

Allosteric
- Regulatory sites, other than the active site of the enzyme that serve to regulate enzymatic activity.

Alpha Helix
- The secondary structure of proteins that is a rod-like, tightly coiled polypeptide chain wound in a
clockwise or counterclockwise direction.

Alpha Keto Acid

- A precursor molecule for amino acid synthesis.

Amino Acid
- A class of 20 organic compounds that combine to form proteins.
- There are 20 common amino acids: alanine, arginine, aspargine, aspartic acid, cysteine, glutamic
acid, glutamine, glycine, histidine, isoleucine, leucine, lysine, methionine, phenylalanine, proline,
serine, threonine, tryptophan, tyrosine and valine.

Aminotransferases
- Enzymes, derived from vitamin B6, that are important in amino acid synthesis.

Antibody
- (AB), also known as an immunoglobulin (Ig), is a large Y-shape protein produced by plasma cells
that is used by the immune system to identify and neutralize foreign objects such as bacteria and
viruses. The antibody recognizes a unique part of the foreign target, called an antigen.

Antigen
- Any substance that causes your immune system to produce antibodies against it. An antigen may
be a foreign substance from the environment, such as chemicals, bacteria, viruses, or pollen.
An antigen may also be formed inside the body, as with bacterial toxins or tissue cells.
 -B-
Beta Sheet
- The secondary structure of proteins where the polypeptide chains are almost completely extended
during the process of folding.

Biuret Test
- Uses a light blue solution which turns purple when mixed with a solution containing protein.
2+
- Usually, Cu and alkali are used to treat compounds containing two or more peptide bonds

2+
that yield a - peptide complex in a base solution. The negative test yields a blue color
Cu
solution for proteins containing fewer than two peptide bonds.

Bovine Insulin
- Or beef insulin, is the first protein to be fully sequenced (by Fred Sanger in 1953).
- It is a two-chain polypeptide hormone produced in vivo in the pancreatic cells and it is the most
studied hormone.

-C-
Cell Motility
- The movement of cells, changes in cell shape including cell division, and the movement of
materials within cells. Proteins link together to form filaments which make movement possible.

Chaperonins
- Are protein molecules that assist the proper folding of other proteins.

Chromoproteins
- Heteroproteins that are coupled with a colored pigment
 o Example: Myoglubin, hemocyanin, cytochromes, flavoproteins, etc.

Coagulated Proteins
- Denatured proteins, formed by the action of heat, x-rays, uv rays, etc.
o Examples: cooked egg albumin, cooked meat, etc.

Coenzyme
- A nonprotein compound that is necessary for the functioning of an enzyme.

Collagen
- The most abundant protein in vertebrates, making up from 25% to 35% of the whole-body protein
content. Collagen fibers are a major portion of tendons, bone and skin. Alpha helices of collagen
make up a triple helix structure giving it tough and flexible properties.

Competitive Enzyme Inhibitors

- Work by preventing the formation of Enzyme-Substrate Complexes because they have a similar
shape to the substrate molecule.

Complete Proteins
- Contain all nine essential amino acids: histidine, isoleucine, leucine, lysine, methionine,
phenylalanine, threonine, tryptophan, and valine.
- Usually animal source are complete proteins.
- Are considered high quality protein, thus digestible and provides sufficient protein to synthesize
nonessential amino acids

Condensation Reaction
- Also commonly referred to as dehydration synthesis.
- It is a chemical reaction in which two molecules or moieties (functional groups) combine to form a
larger molecule, together with the loss of a small molecule. Possible small molecules lost
are water, hydrogen chloride, methanol, or acetic acid but most commonly in a biological reaction it
is water.

Conditionally Essential Proteins

- Proteins that cannot be synthesized due to illness or lack of necessary precursor.

Contractile or Motor Proteins

- These proteins function in the contractile system help in contraction of muscle and cells of our
body. It controls the strength and speed of heart and muscle contractions.
- Responsible for movement.
o Example: Actin, myosin, tubulin, etc.
o Motor proteins are responsible for the undulations of cilia and flagella. Actin and myosin
proteins are responsible for the contraction of muscles.

Covalent Bonds
- Chemical bond that involves the sharing of electron pairs between atoms.

-D-
Defensive Proteins
- These proteins defend against other organisms.
o Example: Antibodies, Fibrinogen, thrombin.

Denaturation
- The process of formation of single stranded DNA from double stranded helical DNA upon heating.
- Alteration of the proteins shape and functions through the use of:
 o Heat
o Acids
o Bases
o Salts
o Mechanical agitation
- Primary structure is unchanged by denaturing.
- Denaturation may be a result of either physical or chemical agents. The physical agents include,
shaking, freezing, heating etc. Chemical agents are like X-rays, radioactive and ultrasonic
radiations.

Deoxyribonucleic acid (DNA)

- A long polymer of nucleotides joined by phosphate groups.
- DNA is the genetic material that provides the blueprint for the proteins that each different cell will
produce in its lifetime.
- It consists of a double stranded helix consisting of a five-sided sugar (deoxyribose) without a free
hydroxyl group, a phosphate group linking the two nucleotides, and a nitrogenous base.

Derived Proteins
- These are proteins that are derived from the action of heat, enzyme or chemical reagents.

DNA polymerases
- Enzymes that create DNA molecules by assembling nucleotides, the building blocks of DNA. These
enzymes are essential to DNA replication and usually work in pairs to create two identical DNA
strands from a single original DNA molecule.

-E-
Electrostatic Interactions
- Are between positive and negative ions of the macromolecules.

Enzymatic Protein
- They are the most varied and highly specialized proteins with catalytic activity. Enzymes catalyze a
variety of reactions.
- Accelerate the metabolic activity in the cells.
o Example: Urease, catalase, cytochrome C, etc.

Enzymes
- A type of protein that acts as a catalyst, speeding up chemical reactions.
- Enzymes can perform their functions repeatedly, functioning as workhorses that carry out the
processes of life.

Enzyme Inhibitor
- Reduce the rate of an enzyme catalyzed reaction by interfering with the enzyme in some way. This
effect may be permanent or temporary.

Epinephrine
- A hormone secreted from the adrenal medulla in response to sympathetic nervous system
stimulation and low blood glucose. Its effects include causing the liver to degrade glycogen into
glucose and decreasing the utilization of glucose by skeletal muscle.

Essential Proteins
- Proteins that must be consumed in a diet.
 -F-
Fibrinogen
- A glycoprotein helps in healing of wounds. It prevents blood loss and inhibits passage of germs.
- A glycoprotein in vertebrates that helps in the formation of blood clots.

Fibroin
- An insoluble protein present in silk created by spiders, the larvae of Bombyx mori, other moth
genera such as Antheraea, Cricula, Samia and Gonometa, and numerous other insects.
- Make the silk spun by spiders and silk worms stronger weight for weight than steel. The soft and
flexible properties come from the beta structure.

Fibrous or Fibrillar Proteins

- Have axial ratio more than 10, hence, resemble long ribbons or fibres in shape.
- They are mostly found in animals, and are not soluble in water or in solution of dilute acids.
- Aid in protection and structural support.
o Example: Collagen, Keratin, Elastins, Fibroin.

Folins Test
- This is a specific test for tyrosine amino acid, where blue color develops with
phosphomolybdotungstic acid in alkaline solution due to presence of phenol group.

-G-
Gel electrophoresis
- A method for separation and analysis of macromolecules (DNA, RNA and proteins) and their
fragments, based on their size and charge.

Gene Therapy
- The replacement of a defective gene in an organism suffering from a genetic disease. Recombinant
DNA techniques are used to isolate the functioning gene and insert it into cells. More than 300
single-gene genetic disorders have been identified in humans. A significant percentage of these
may be amenable to gene therapy.

Genome
- Genetic material of an organism.
- It is encoded either in DNA or, for RNA viruses, in RNA. The genome includes both the genes and
the non-coding sequences of the DNA/RNA.

Genomics
- A discipline in genetics that applies recombinant DNA, DNA sequencing methods, and
bioinformatics sequence, assemble, and analyze the function and structure
of genomes (the complete set of DNA within a single cell of an organism).

Gluconeogenesis
- The process of synthesizing glucose from non- glucose precursors such as amino acids.

Globular or Corpuscular Proteins

- Have axial ratio less than 10.
- They are compactly folded and coiled and possess a relatively spherical or ovoid shape.
 - They are usually soluble in water and in aqueous media.
o Example: Insulin, plasma albumin, globulin enzymes.

Globulins
- Holoproteins and are a family of globular proteins that have higher molecular
weights than albumins.
- Insoluble in pure water but soluble in dilute salt solutions.

Glycoproteins
- Heteroproteins that contain carbohydrates as the prosthetic group.
- Contain oligosaccharide chains (glycans) covalently attached to polypeptide side-chains. The
carbohydrate is attached to the protein in a cotranslational or posttranslational modification.
o Examples: egg albumin, serum globulins, serum albumins

-H-
Hemoglobin
- The oxygen carrying component of blood, made up of two polypeptide chains, one with 141 amino
acids and the other is a different type of 146 amino acids.
- The protein molecule in red blood cells that carries oxygen from the lungs to the body's tissues and
returns carbon dioxide from the tissues back to the lungs. Hemoglobin is made up of four protein
molecules (globulin chains) that are connected together.

Heteroproteins or Conjugated or Complex Proteins

- Proteins that are made of amino acids and other organic compounds.

Histones
- Holoproteins that are found in the nuclei of eukaryotic cells responsible for DNA folding and
chromatin formation.
- Occurs only in animals and are basic proteins.
- Possess simple structure and low molecular, are water soluble and are not coagulated by heat.
- Strongly basic in character due to the high content of lysine, arginine.
o Example: nucleoshistones, globin

Holoproteins or Simple Proteins

- Made of only one type of amino acid, as structural component, on decomposition with acids, they
liberate constituent amino acids.
- Mostly globular type of proteins except for scleroproteins, which are fibrous in nature.

Hopkins- Cole Test

- Also known as Glyoxylic Acid Test, for the presence of the indole group.
- When strong acid is added to an amino acid containing the indole group like tryptophan, a violet
colored complex will be formed.

Hormonal Proteins
- Helps in the coordination of an organisms activities.
o Example: Insulin, a hormone secreted by the pancreas, causes other tissues to take up
glucose, thus regulating blood sugar concentration.

Hormones
- Proteins based chemicals that are secreted by the endocrine glands.
- Chemical messengers that transmit signals from one cell to the other.
Hydrogen Bond
- The attractive force between the hydrogen attached to an electronegative atom of one molecule
and an electronegative atom of a different molecule. Usually the electronegative atom is oxygen,
nitrogen, or fluorine, which has a partial negative charge.

Hydrolysis
- From the Greek word hydro-, meaning "water", and lysis, meaning "separation"
- A reaction involving the breaking of a bond in a molecule using water. The reaction mainly occurs
between an ion and water molecules and often changes the pH of a solution.
- Refers to the breaking of the peptides bonds that connect amino acids to compose a protein.
Strong acid solution is used to hydrolyze proteins. Inside our body, hydrolysis takes a faster rate
because of the help of hydrolyzing enzymes.

Hydrolytic Decomposition of Proteins

- Successive stages from protein molecule into amino acid:

Hydrophilic Amino Acids

- Arrange themselves outside the molecule.

Hydrophobes
- Non-polar molecules and usually have a long chain of carbons that do not interact with water
molecules.

Hydrophobic Amino Acids

- Tend to arrange themselves inside the molecule.

Hydrophobic Collapse
- The process whereby water-fearing protein side chains interact more favorably with themselves
than with water to create a hydrophilic exterior.

Hydrophobic Interactions
- The relations between water and hydrophobes (low water-soluble molecules).

-I-
Immunomodulators
- A diverse class of proteins that boost the immune system. Many are cell growth factors that
accelerate the production of specific cells that are important in mounting an immune response in
the body. These proteins are being investigated for use in possible treatments for cancer.

Incomplete Proteins
- Low in one or more essential amino acid.
- Usually plant sources are incomplete, except soy.

Isoelectric Point
- The pH at which a particular molecule carries no net electrical charge.
 -K-
Keratin
- A tough insoluble protein that makes up the quills of echidna, human hair and nails, and the rattle of
a rattle snake. The structure comes from alpha helices that are cross-linked by disulfide bonds.

Ketogenic
- The process whereby fatty acids are broken down to produce ketones.

Krebs Cycle
- Also known as the Citric Acid Cycle, the Krebs Cycle consists of a series of reactions that produce
high-energy electron carriers to be used in the electron transport chain in the production of
adenosine triphosphate (ATP).

Kwashiorkor
- It is a form of severe proteinenergy malnutrition generally the result of a diet high in grains and
deficient in protein.
- Characterized by edema; irritability; anorexia; ulcerating dermatoses; muscle tone and strength
diminish; hair is brittle and easy to pull out; appear pale, sad, and apathetic; prone to infection,
rapid heart rate, excess fluid in lungs, pneumonia, septicemia, and water and electrolyte
imbalances; and an enlarged liver with fatty infiltrates.

-L-
Levinthal's Paradox
- The difference between the actual and theoretical times of protein folding.

Lipoproteins
- Heteroproteins wherein proteins form complexes with lipids.
- A biochemical assembly that contains both proteins and lipids, bound to the proteins, which allow
fats to move through the water inside and outside cells. The proteins serve to emulsify the lipid
molecules.
o Example: lipovitellin, lipoproteins of blood.

-M-
Marasmic Kwashiorkor
- It is a mixed form of both marasmus and kwashiorkor and is characterized by the presence of both
wasting and bilateral pitting oedema.
- A malnutrition disease, primarily of children, resulting from the deficiency of both calories and
protein. The condition is characterized bysevere tissue wasting, dehydration, loss of subcutaneous
fat, lethargy, and growth retardation.

Marasmus
 - It is a form of severe malnutrition characterized by energy deficiency.
- Symptoms include:
o Frail, emaciated appearance
o Weakened and appear apathetic
o Many cannot stand without support
o Look old
o Hair is thin, dry, and lacks sheen
o Body temperature and blood pressure are low
o Prone to dehydration, infections, and unnecessary blood clotting

Metal Ion Coordination

- Important in Tertiary Structure of proteins. Two side chains with the same charge would normally
repel each other. However, if a metal is placed between them, they will coordinate to the metal and
be connected together.

Metalloproteins
- Heteroproteins that are linked with various metals.
o Example: casein, collagen, ceruloplasmin, etc.

Metaproteins
- Derived in the later stages of protein hydrolysis by slightly stronger acid or alkalis.
o Example: acid and alkali metaproteins

Millons Test
- Test to recognize the presence of the hydroxyphenyl group in proteins like those present in the
amino acid, tyrosine. The reaction between the protein and mercury forms a white precipitate which
turns red upon heating.

Mucoproteins
- Heteroproteins that contain carbohydrates as the prosthetic group.
- A glycoprotein composed primarily of mucopolysaccharides. It can be found throughout the body,
including the Gastrointestinal tract, reproductive organs, airways, and the synovial fluid of the
knees.
o Examples: Ovomucoid, mucin etc.

Multipotent Cells
- Can develop into more than one cell type, but are more limited than pluripotent cells; adult stem
cells and cord blood stem cells are considered multipotent.

-N-
Native Proteins
- The concept of a protein in its natural state, in the cell, unaltered by heat, chemicals, enzyme
action, or the exigencies of extraction.

Ninhydrin Test
- A very widely used reaction to detect the free amino group in amino acids.
- In this test, proteins must be heated first to digest or hydrolyze and make the amino acids free.
Ninhydrin reacts with the free alpha amino group yielding a deep blue color solution. Proline and
hydroxyproline do not give the characteristic color reaction; instead a yellow color is produced.

Nitrogen Pool
- Or Amino Acid Pool, is a grand mixture of amino acids available in the cell derived from dietary
sources or the degradation of protein.
Non-competitive Enzyme Inhibitors
- Work not by preventing the formation of Enzyme-Substrate Complexes, but by preventing the
formation of Enzyme-Product Complexes. So they prevent the substrate from reacting to form
product.

Non-essential Proteins
- Proteins that can be synthesized in the body.

Non-polar
- As opposed to polar, Referring to the hydrophobic or "water fearing" qualities of amino acids.

Neurotransmitter
- Proteins responsible for transmission of the electrical potential across a synapse between nerves.

Nucleoproteins
- Heteroproteins. These are compounds containing nucleic acids and proteins.
o Example: Nucleoproteins, nucleohistones, nuclein.

Nutrient and Storage Proteins

- These proteins provide nutrition to growing embryos and store ions.

-O-
Oxaloacetate
- A four-carbon molecule found in mitochondria that condenses with acetyl CoA to form citrate in the
first reaction of the Krebs Cycle. Oxaloacetate must be constantly regenerated in order for the
Krebs Cycle and the electron transport chain to continue.
 -P-
Peptides
- Compounds containing two or more amino acids. They may be dipeptide, tripeptide, tetrapeptide or
polypeptide.
- Water soluble, are not coagulated by heat and are precipitated by phosphotungstic acid.

Peptones
- It is a further hydrolyzed stage than the proteoses.
- Soluble in water and are not coagulated by heat and are not precipitated by ammonium sulphate.
They are precipitated by phosphotungstic acid.

Phenylketonuria
- The disease state in which an individual has a defect in phenylalanine metabolism.

Phosphoproteins
- Heteroproteins that are linked with phosphoric acid.
o Example: casein.

pKA
- The pKa is an intrinsic property of a compound defined as the ability to release protons into
solution.

Pluripotent Cells
- Having the capacity to become any kind of cell or tissue in the body. Embryonic stem cells and cells
of the inner cell mass are pluripotent. Adult stem cells are multipotent. The mammalian embryo
(blastocyst trophoblast plus inner cell mass) is totipotent because it can become an entire
organism. Fully differentiated cells from many plants are totipotent.

Polar
- As opposed to non-polar, referring to the hydrophilic or "water loving" qualities of amino acids.

Polypeptides
- Multiple amino acids joined by peptide bonds.

Primary Derived Proteins

- Derivatives of proteins, in which the size of the protein molecule is not altered materially.
- Denatured or coagulated proteins which are produced by the action of heat, x-ray, uv rays, vigorous
shaking, acid or alkali. Their molecular weight is same as native protein, but they differ in solubility,
precipitation and crystallization.

Primary Structure
- The first level of protein structure that is simply the linear sequence of its constituent amino acids
that make up the polypeptide chain, and thus determines the proteins properties.

Prosthetic Groups
- Non-amino acid group.
- A tightly bound, specific non-polypeptide unit required for the biological function of some proteins.
- May be organic (such as a vitamin, sugar, or lipid) or inorganic (such as a metal ion), but is not
composed of amino acids.
- Bound tightly to proteins and may even be attached through a covalent bond, as opposed to
coenzymes, which are loosely bound. In enzymes, prosthetic groups are often involved in
the active site, playing an important role in the functions of enzymes.

Protamine
- Small, arginine-rich, nuclear proteins that replace histones late in the haploid phase
of spermatogenesis and are believed essential for sperm head condensation
and DNA stabilization.
- Holoproteins, occurs only in animals and are basic proteins.
- Possess simple structure and low molecular, are water soluble and are not coagulated by heat.
- Strongly basic in character due to the high content of lysine, arginine.
 o Example: salmine, clupine, cyprinine
Proteans
- Derived in the early stage of protein hydrolysis by dilute acid, enzyme or alkali
o Example: fibrin from fibrinogen

Proteome
- The entire set of proteins expressed by a genome, cell, tissue or organism at a certain time.

Proteomics
- It is the large-scale study of proteins, particularly their structures and functions.

Protein
- Derived from the Greek word, proteios which means pre-eminent or first, and known as the
building blocks of life. Proteins are vital parts of living organisms, as they are the main components
of the physiological metabolic pathways of cells.
- Complex, specialized and most abundant molecules in cells (50% or more of the dry weight of
cells) composed of more than 50 amino acids.

- Characteristics:
o Proteins are organic substances, made up of nitrogen and also, oxygen, carbon and
hydrogen.
o Proteins are made up of amino acids.
o Proteins are the most important biomolecules, they are the fundamental constituent of the
cytoplasm of the cell.
o Proteins are the structural elements of body tissues.
o Proteins give heat and energy to the body and also aid in building and repair.
o Proteins like enzymes are functional elements that take part in metabolic reactions.
o Only small amounts of proteins are stored in the body as they can be used up quickly on
demand.
o Proteins have a molecular weight of 5 to 300 kilo-daltons.

- Physical Properties:
o Proteins are colorless and tasteless.
o They are homogeneous and crystalline.
o Proteins vary in shape, they may be simple crystalloid structure to long fibrilar structures.
o Protein structures are of two distinct patterns - Globular proteins and fibrilar proteins.
o In general proteins have large molecular weights ranging between 5 X 103 and 1 X 106.
o Due to the huge size, proteins exhibit many colloidal properties, e.g. Tyndall Effect.
o The diffusion rates of proteins is extremely slow.
o Proteins tend to change their properties like denaturation. Many times the process of
denaturation is followed by coagulation.
o Proteins like the amino acids exhibit amphoteric property i.e., they can act as acids and
alkalis. As the proteins are amphoteric in nature, they can form salts with both cations and
anions based on the net charge.
o The solubility of proteins depends upon the pH. Lowest solubility is seen at isoelectric
point, the solubility increases with increase in acidity or alkalinity.
o All the proteins show the plane of polarized light to the left, i.e., laevorotatory.

- Chemical Properties:
o Proteins when hydrolyzed by acidic agents, like conc. HCl yield amino acids in the form of
their hydrochlorides
o Proteins when are hydrolyzed with alkaline agents leads to hydrolysis of certain amino
acids like arginie, cysteine, serine, etc., also the optical activity of the amino acids is lost.
o Proteins with reaction with alcohols gives its corresponding esters. This process is known
as esterification.
o When free amino acids or proteins are said to react with mineral acids like HCl, the acid
salts are formed.
Protein Digestion

Protein-Energy Malnutrition (PEM)

- Or proteincalorie malnutrition, refers to a form of malnutrition where there is inadequate
calorie or protein intake.
- Protein is used for energy rather than its other functions in the body.
- Other important nutrients are in short supply.
- More prevalent in infants and children.

Protein Metabolism
- Denotes the various biochemical processes responsible for the synthesis of proteins and amino
acids, and the breakdown of proteins (and other large molecules, too) by catabolism.
Protein Quality
- A term used to describe how well a protein from food matches the body's requirements and,
therefore, how useful the protein is for our body. It is determined by digestibility and types and
amounts of amino acids.

Protein Superfamily
- It is the largest grouping (clade) of proteins for which common ancestry can be inferred. Usually
this common ancestry is based on structural alignment and mechanistic similarity even though no
sequence similarity is evident.

Protein Synthesis
- The process by which amino acids are linearly arranged into proteins through the involvement of
ribosomal RNA, transfer RNA, messenger RNA, and various enzymes.

Protein Turnover
- The continual degradation and synthesizing of protein.
- It is the balance between protein synthesis and protein degradation.

Proteolysis
- The breakdown of proteins into smaller polypeptides or amino acids by hydrolysis.

Proteoses
- Formed by the action of pepsin or trypsin.
- Soluble in water and are not coagulated by heat. They are precipitated by heat.
 o Examples: albumose from albumin, globulose from globulin

Pyruvate
- Pyruvate is a three-carbon compound formed through the degradation of glucose via glycolysis.
Two pyruvate molecules are formed per molecule of glucose that enters glycolysis.

-Q-
Quaternary Structure
- The fourth level of protein structure that refers to the spatial arrangement of the subunits within the
protein.
- Some proteins contain more than one polypeptide chains, this association of polypeptide chains
refers to the quaternary structure.

-R-
Receptor Proteins
- Located on the outer part of the cells, they control the substances that leave and enter the cell.
- Function: Response of cell to chemical stimuli
o Example: Receptors built into the membrane of a nerve cell detect signaling molecules
released by other nerve cells.

Regulatory Proteins
- They regulate cellular or metabolic activities.
o Example: Insulin, G proteins, etc.

Renaturation or Renaturization
- The process of formation of double stranded DNA (reannealing) from single stranded DNA upon
cooling.
- The process by which proteins or complementary strands of nucleic acids re-form their native confo
rmations.

Ribonucleic acid (RNA)

- RNA is a long polymer of ribose (a five-sided sugar with a free hydroxyl group) and nitrogenous
bases linked via phosphate groups
- It is complementary to one of the DNA strands and forms the proteins that are specified by the cell.

-S-
Sangers Reaction
- Proteins react with FDNB (1-fluoro-2,4-dinitrobenzene) reagent to produce yellow colored
derivative, DNB amino acid.

Salt Bridges
 - Actually a combination of two noncovalent interactions: hydrogen bonding and electrostatic
interactions. This is most commonly observed to contribute stability to the entropically unfavorable
folded conformation of proteins.

Scleroproteins or Albuminoids
- Holoproteins that occur mostly in animals and are commonly known as animal skeleton proteins.
- They are insoluble in water, and in dilute solution of acids, based and salts.

Secondary Derived Proteins

- Hydrolysis occurs, as a result the molecules are smaller than the original proteins.
- Formed by the progressive hydrolysis of proteins at their peptide linkage.
- They represent a great complexity with respect to their size and amino acid complexity.

Secondary Structure
- The second level of protein structure where the linear sequence of proteins begins to fold into
regular repeating patterns.
- The regular pattern is due to the hydrogen bond formation between atoms of the amino acid
backbone of the polypeptide chain.
- The most common types of the secondary structure are the alpha helix and the beta pleated sheet.

Sickle Cell Disease

- An inherited blood disorder, results from a single amino acid substitution in the protein hemoglobin.

Storage Proteins
- Store mainly mineral ions in the body, like potassium, iron etc.
o Examples: Casein, the protein of milk, is the major source of amino acids for baby
mammals. Plants have storage proteins in their seeds. Ovalbumin is the protein of egg
white, used as an amino acid source for the developing embryo.

Structural Proteins
- These proteins aid in strengthening or protecting biological structures.
o Example: Collagen, elastin, keratin, etc.
 o Keratin is the protein of hair, horns, feathers, and other skin appendages. Insects and
spiders use silk fibers to make their cocoons and webs, respectively. Collagen and elastin
proteins provide a fibrous framework in animal connective tissues.

Substrates
- A molecule that an enzyme binds to preferentially with high affinity.
Subunit
- Called to each polypeptide chain. The subunits can be same or different ones.

Sulfur Test
- Few amino acids containing sulfur such as methionine, cysteine and cystine (oxidized cysteine) can
be tested using lead acetate paper. The reaction between
H2 S gas and lead acetate paper
yields to lead (II) sulfide producing a brown or black color on the lead acetate paper.

-T-
Tertiary Structure
- The third level of protein structure where side chain interactions dictate the direction of the folding.
- Three dimensional structure formed by the bending and twisting of the polypeptide chain.
- The linear sequence of polypeptide chain is folded into compact globular structure. The folding of
the polypeptide chain is stabilized by weak, noncovalent interactions. These interactions are
hydrogen bonds and electrostatic interactions.
- Hydrophobic interactions, disulphide linkages and covalent bonds also contribute to tertiary
structure.

- Formed by the following interactions:

o Covalent Bonds
o Hydrogen Bonding
o Salt Bridges
o Hydrophobic Interactions
o Metal Ion Coordination

Totipotent Cells
- Can form all the cell types in a body, plus the extraembryonic, or placental, cells. Embryonic cells
within the first couple of cell divisions after fertilization are the only cells that are totipotent.

Toxic Proteins
- These proteins hydrolyze or degrade enzymes.
o Example: snake venom, ricin.

Transamination
- The synthesis of amino acids in the liver.

Transport or Carrier Proteins

- These proteins help in transport of ions or molecules in the body.
o Example: Myoglobin, hemoglobin, etc.

-X-
Xanthoproteic Acid
- Noncrystallizable yellow substance derived from proteins upon treatment with nitric acid.

Xanthoproteic Test
- Boiling proteins with conc. HNO3, yellow color develops due to presence of benzene ring.
- A method that can be used to determine the amount of protein soluble in a solution, using
concentrated nitric acid.
- The test gives a positive result in those proteins with amino acids carrying aromatic groups,
especially in the presence of tyrosine. If the test is positive the proof is neutralized with an alkali,
turning dark yellow. The yellow colour is due to xanthoproteic acid which is formed due
to nitration of certain amino acids, most common examples being tyrosine and tryptophan. This
chemical reaction is a qualitative test, determining the presence or absence of proteins.

Xanthoprotein
- is a yellow acid substance formed by the action of hot nitric acid on albuminous or protein matter
and is changed to a deep orange-yellow colour by the addition of ammonia. The colour reaction is
used to identify such proteins in the Xanthoproteic Test.

-Z-
Zwitterions
- Amino acids in a form of neutrality where the carboxyl group and amino group are ready to donate
and accept protons, respectively.
- Compound where both a positive charge and a negative charge exist on the same molecule. In
solution their form changes depending on the Ph.