aims to understand how the lifeless molecules interact to make the complexity and efficiency of the life phenomena and to explain the diverse forms of life in chemical terms

structure-function relationship for proteins, carbohydrates, DNA/RNA, lipids, etc.;

totality of chemical reactions that occur in living organism, concerning catabolism & anabolism of building blocks, as well as management of cellular Energy;

DNA replication and protein synthesis.

CONTAIN ENZYME PAPAIN

•          CONTAIN PROTEOLYTIC ENZYME BROMELAIN

CONTAIN AMYLASES AND GLUCOSIDASES

Composed only of simple protein

Major types of biomolecules found in all types of living organisms

were the last of these to be isolated, in 1868, by Johann Friedrich Miescher, a Swiss, twenty-four years old.

describes the properties of biomolecules.

applies the techniques of physics to study the structures of biomolecules.

increasingly seeks to understand disease states in molecular terms.

illuminated metabolism by describing the dietary requirements for maintenance of health.

shown that single-celled organisms and viruses are ideally suited for the elucidation of many metabolic pathways and regulatory mechanisms.

investigates life processes at the tissue and organism levels.

describes the biochemical division of labor within a cell.

describes mechanisms that give a particular cell or organism its biochemical identity

are the basic structural and functional life units where biomolecules are produced (and degraded) and function, with thousands of biochemical reactions occur in regulated ways

is extremely versatile in forming covalent bonds with other atoms or itself

is a globular protein with four polypeptide chains (tetrameric)

disease due to deficiency of vitamin C which is important coenzyme for conversion of proline into hydroxyproline and lysine into hydroxylysine. Thus, synthesis of collagen is decreased leading to abnormal bone development, bleeding, loosing of teeth and swollen gum.

proteins conjugated with sugar (carbohydrate)

These are proteins conjugated with lipids.

These are proteins conjugated with phosphate group. Phosphorus is attached to OH group of serine or threonine.

These are the rest of amino acids that are formed in the body in amount enough for adults and children.

These are formed in the body but not in sufficient amount for body requirements especially in children

These amino acids can’t be formed in the body and so, it is essential to be taken in diet. Their deficiency affects growth, health and protein synthesis.

is alkyl hydrophobic group which can’t enter in hydrogen bond formation

in which R contains polar hydrophilic group so can forms hydrogen bond with H₂O.

at physiological pH will carry negative charge.

Contain two or more NH₂ groups or nitrogen atoms that act as base i.e. can bind proton.

proteins that direct and regulate metabolism in the body, contractile muscle permit movement, collagen forms a framework.

are the building units of proteins.

the most abundant and functionally diverse molecules in living system. Virtually every life process depends on this class of molecules.

Inherited disease resulting from genetic deficiency or mutation in gene that synthesizes collagen type I leading to abnormal bone formation in babies and frequent bone fracture in children. It may be lethal.

is a chronic obstructive lung disease (obstruction of air ways) resulting from deficiency of α1-antitrypsin particularly in cigarette smokers.

is a fibrous protein of three polypeptides (trimeric) that are supercoiled like a rope.

Group of molecules that possess a protein core and a side chain of sugars; are formed of Glycosaminoglycans (GAGs) covalently attached to the core proteins, found in all connective tissues, ECM or extracellular matrix and on the surface of many cells

These are the fundamental structures, bricks and mortar of protein architecture.; By means of arranging these FUNDAMENTAL structural elements in DIFFERENT combinations,

;WIDELY DIVERSE PROTEINS can be constructed.

These are structure of complex PROTOPORPHYRIN IX and FERROUS IRON

These are family of disorders caused by production of structurally abnormal hemoglobin molecules

is decreased or absent ,normal α chains α chains cant form stable tetramers thus precipitate , causing premature death of cell(destined to be matured RBC) Minor if only one gene is affected, major if both are affected Minor  do not require specific treatment.

Composed of protein and a prosthetic group

Proteins that form an active enzyme system

-Apo enzyme + cofactor

-Catalytically active enzyme

-also known as a Cofactor

-Non-protein part of a conjugated enzyme

-provide additional chemically reactive functional groups besides those present in the amino acids of the apoenzymes

A substance that slows down or stops the normal catalytic function of an enzyme by binding to the enzyme

• Resembles the substrate

• Inhibitor competes with the substrate for binding to the active site of the enzyme

• If an inhibitor is bound to the active site:

Prevents the substrate molecules to access the active site

• Decreasing / stopping enzyme activity

• The binding of the _______ to the active site is a reversible process

• Add much more substrate to outcompete the _______

•          Inhibit histidine decarboxylase, an enzyme which converts histidine to histamine

• –Permanently deactivates the enzyme

do not resemble substrates

have a quaternary structure

•          Are composed of 2 or more protein chains

•          Possess 2 or more binding sites

is a combination of  ACE and calcium blocker

• β-lactam antibiotics inhibit transpeptidase

• -Transpeptidase enzyme strengthens the cell wall

• Forms peptide cross links between polysaccharides strands in bacterial cell walls

• –Without transpeptidase enzyme >>> weakened cell wall, bacteria die

are proenzyme -requires a biochemical change (*Golgi bodies) to become an active form

•          is normally not found in high levels in blood, as it is produced in cells

One binding site for the substrate

second binding site for the regulatory molecule

is used to measure kidney function

It is also known as a minor hemoglobin synthesized in adult at low levels.

-Most abundant form of glycosylated hemoglobin;

-Increased level in red blood cells are found in patients with DM

-A fetal hemoglobin

-This comprises the 60% of total hemoglobin in the erythrocytes of a fetus.

due to an altered amino acid sequence

-A genetic disorder of the blood

-A hereditary hemolytic disease

-imbalance occur in the synthesis of globin chains

-The MOST common single gene disorder in humans.

Oxidation of the HEME group to the Ferric state forms methemoglobin, which CANNOT bind OXYGEN

-Some beta globin chain has the sickle cell mutation

-Others carry mutation from HBC

–due to an altered amino acid sequence

-has a single amino acid substitution in the sixth position of the globin chain.

iron overload

is secreted by the cell into the extracellular space that tend to interacts with specific glycoprotein microfibrils (fibrillin).