ALTHEA V.

DESAMPARADO Nucleus-Control center of the cell

BSN-1B Cytoplasm-Jelly-like substance enclosed by cell
membrane and contains organelles
BIOCHEMISTRY 1 NOTES
Ribosomes-Site of protein synthesis
Golgi Bodies-Package molecules from ER for
CELL STRUCTURE
storage or transport out of cell
Matthias Schleiden- Cell is the unit of
Nucleolus-Dark stained bodies in the nucleus
structure in plants.
which makes ribosomes that make proteins
Lynn Margulis- Discovered the chloroplast and
Mitochondria-Powerhouse of the cell
mitochondria contains their own DNA.
Rudolf Virchow-Cell came from pre-existing
cell. INTRODUCTION TO BIOCHEMISTRY
Theodore Schwann-Cells are the unit of Biochemistry - Chemistry of Living beings or
structure in animal cells. Chemical Basis of Life.
Robert Hooke-Coined the term cell. - Hundreds of Biochemical reactions and
Biochemical processes
- Occurring in sub cellular organelles of a cell in
Nuclear Envelope-Double membrane that
an organized manner.
separate the nucleus from the cytoplasm
- Study of Biochemical Reactions and Processes
Smooth Endoplasmic Reticulum-Lacks
ribosome on its surface and performs lipid Branches of Biochemistry
synthesis, carbohydrates metabolism and
Medical Biochemistry-Deals with chemical
detoxification
basis of human body.
Lysosomes-Contains digestive enzymes
Clinical Biochemistry-Deals with clinical
Vacuole-Fluid-filled sacks for storage diseases/pathological conditions of human body
Cell Wall-Found outside the cell membrane of Clinical Biochemistry supports:
the plant cell
Diagnosis, Therapy and Research of Medical
Cell Membrane-Composed of double layer of field.
phospholipids and proteins which protects the
Bacterial Biochemistry-Deals with Microbes.
cell from the outside environment
Plant Biochemistry- Deals with Plants.
Rough Endoplasmic Reticulum- Has
ribosomes on its surface which makes Animal Biochemistry-Deals with animals
membrane proteins and export out of cell
Industrial Biochemistry-Deals with industrial
Centrioles-Found only in animal cells which products involved with microorganisms.
plays an important role in organizing mitotic
spindle during cell division
Cilia-Hair like structures which are sort and
numerous on the surface of the cell
Historical Developments of Biochemistry Isolation and Structural elucidation of
Biomolecules.
- Biochemistry emerged in the late 18th and
early 19th century. Understand completely all the organized
Biochemical processes
- The term Biochemistry was first introduced by
the German Chemist Carl Neuberg in 1903. Occurring in living cells at the molecular/sub
cellular level.
- In the 1940s Clinical Biochemistry evolved, as
an autonomous field Identification of disease mechanisms:
Pioneer Workers and their Discovery/Work Study of Inborn Errors of metabolism.
Berzilus-Enzymes Catalysis Study of Oncogenes in cancer cells.
Edward Buchner-Enzyme Extraction
Louis Pasteur-Fermentation Process BIOMOLECULES
Lohmann-Role of Creatine PO4 in muscles - We call these C-containing compounds as
organic compounds.
Hans Kreb-TCA Cycle
Basic forms of carbons
Banting and Macleod-Insulin
Hydrocarbon- organic compounds that contain
Fiske and Subbarow-Role of ATPs
only carbon and hydrogen
Watson and Crick-Double Stranded DNA
Hydroxyl group- hydrogen bonded to oxygen (-
Landsteiner-Protein Structure OH) may be bonded to a parent carbon chain

Peter Mitchell-Oxidative Phosphorylation Functional group- are specific arrangement of

atoms within an organic molecules and which
Nirenberg-Genetic Code on Mrna impart the physical properties and chemical
Paul Berg-Recombinant DNA Technology reactiy of the molecule in which they found

Karry Mullis-Polymerase Chain Reaction Biomolecules-are molecules that is present in

living organisms, including large
Khorana-Synthesized Gene macromolecules such as proteins, carbohydrates,
lipids, and nucleic acids.
Aim and Objectives to Study Biochemistry
Macromolecule-“Large molecule”
To know the various Biomolecules composed in
Human body: - Made from carbon (C) compounds
Chemistry/Structure Monomers- small subunits or ‘building blocks’
Occurrence/Location Polymers-large units composed of multiple
monomers
Functions/Role
Intermolecular forces - They are the central to
Determination of mode of action of
the most critical process in living organisms
Biomolecules is by:
such as protein conformation, enzymes activity,
and nucleic acid-base pairing.
The Four Macromolecules and Their Lipids-Function as Membrane
Functions
-Are organic molecules that are insoluble in
Carbohydrates-Stores energy water because of many polar and H- bonding
functional group
- Chain of organic molecule with 1:2:1 mole
ratio of carbon, hydrogen and oxygen (CH2O) -Have very high proportion of carbon- hydrogen
bonds
- Acts as energy storage or food reserves in
plants and animals When placed in water, lipid molecules cling
together, exposing their polar groups to
- A highly polar molecules because of
surrounding water molecules, the nonpolar
abundance of -OH groups in its structure
groups stays within the interior of the lipid
Classification of Carbohydrates cluster

1. Simple Carbohydrates (sugar) Nucleic Acid-Contain Genetic information

-small and easily decomposed into its basic units - Made up of repeating units of monomers
known as nucleotides (sugar, phosphate, and
-provide instant source of energy nitrogenous bases)
-Simple sugars are monosaccharides and
disaccharides
PROTEINS AND AMINO ACIDS
2. Complex Carbohydrates
Proteins- is found throughout the body-in
-serve as structural materials for cells muscle, bone, skin, hair, and virtually every
-composed of simple carbohydrates covalently other body part or tissue
bonded to each other - Proteins are made up of many building blocks,
-Complex sugars are polysaccharides. known as amino acids.

Proteins-Do Chemistry in the Cells Type of Proteins

-Are complex molecules composed of one or Enzymatic proteins-Selective acceleration of

more amino acids linked by peptide bonds chemical reactions

-Peptide Bonds- type of covalent bond Structural proteins- Support

-Amino Acid- building blocks of protein Storage proteins- Storage of amino acids

Hemoglobin is a protein found in the blood cells Transport proteins-Transport of other

and is used to carry oxygen substances

Insulin, the protein that regulates metabolism, is Hormonal proteins-Coordination of an

only made up of 51 amino acids organisml’s activities

Keratin is a structural protein found in hair, Receptor proteins- Response of cell to

skin, and nails. chemical stimuli

Fibroin / Silk protein - Fibroin is found in silk. Contractile and motor proteins-Movement
Silk has a smooth and soft texture Defensive proteins-Protection against disease
Levels of Protein Structure
Primary structure - the sequence of amino 9 amino acids are non-polar ( glycine, alanine,
acids in the peptide chain and the location of the valine, leucine, isoleucine, phenyl alanine,
disulfide bridges. tryptophan, proline and methionine).
Secondary structure - a description of the
The twenty common amino acids are often
conformation/ shape of the backbone of the
referred to using three-letter abbreviations. The
protein.
structures, names, and abbreviations for the
Tertiary structure - a description of the 3D twenty common amino acids are shown below.
structure of the entire polypeptide. Note that they are all α-amino acids.
- If the protein has more than one chain it can - Each amino acid, aside from its name, has a
have a quaternary structure. three letter abbreviation and a one letter code.
Amino Acids are the building units of proteins.
There are about 300 amino acids occur in nature.
Only 20 of them enter in proteins synthesis.
Structure of amino acids:
Four different groups are attached to α- carbon:
• amino group
• COOH group
• Hydrogen atom
• and side Chain (R).
An amino acid is a compound having both a
carboxyl group(-COOH) and an amino
Functions of Amino Acids
group(-NH2).
Apart from being the monomeric constituents of
Polar amino acids: in which R contains polar
proteins and peptides, amino acids serve variety
hydrophilic group so can forms hydrogen bond
of functions.
with H2O. In those amino acids, R may contain:
(a) Some amino acids are converted to
OH group : as in serine, threonine and tyrosine
carbohydrates and are called as glucogenic
- SH group : as in cysteine amino acids.

Amide group: as in glutamine and aspargine (b) Specific amino acids give rise to specialised
products, e.g.
NH2 group or nitrogen act as a base (basic
amino acids ): as lysine, arginine and histidine • Tyrsione forms hormones such as thyroid
hormones, epinephrine and norepinephrine
COOH group (acidic amino acids): as aspartic and a pigment called melanin.
and glutamic .
• Tryptophan can synthesize a vitamin called
Non polar amino acids: R is alkyl hydrophobic niacin.
group which can’t enter in hydrogen bond
formation.
• Glycine, arginine and methionine synthesize Enzymes are biological catalysts that increase
creatine. the reaction rate of biochemical reactions.
Glycine and cysteine help in synthesis of Bile Characteristics of enzymes
salts.
A. Made of proteins (or RNA).
•Glutamate, cysteine and glycine synthesis
B. They are very specific and only work with a
glutathione.
certain set of reactants or substrates that fit on
•Histidine changes to histamine on their active site.
decarboxylation.
C. Enzymes can be used over and over again.
• Serotonin is formed from tryptophan.
D. When an enzyme binds with the substrate, the
• Glycine is used for the synthesis of haem. substrate interacts with the enzyme causing it to
change shape. This change in shape facilitates
• Pyrimidines and purines use several amino
the chemical reaction to occur. This is called the
acids for their synthesis such as aspartate and
induced fit.
glutamine for pyrimidines and glycine, aspartic
acid, Glutamine and serine for purine synthesis Ribonuclease decomposes RNA, and the
nucleotides can be recycled.
c) Some amino acids such as glycine and
cysteine are used as detoxicants of specific The purple part is the enzyme; the green part is
substances. the substrate (RNA).
(d) Methionine acts as “active” methionine (S-
adenosylmethionine) and transfers methyl group
to various substances by transmethylation.
(e) Cystine and methionine are sources of
Sulphur

ENZYMES
Energy Activation
- If you mix two moles of hydrogen gas H2 with
one mole of oxygen gas-nothing happens.
If you add a spark to the container, the following
reaction occurs. KABOOM
2H2 + O2  2 H2O G= -58 kcal/mole
- In order for water to be produced H2 must
become 2H and the O2 must become 2O as this
frees up the electrons tied up in covalent bonds,
to form chemical bonds forming water, H2O.
- The energy used to break the bonds in the
reactants so they can be reformed in the products
is called the energy of activation.