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Chapter 2 - The Chemicals Components of The Cells

The document discusses the chemical components of cells, focusing on the types of chemical bonds, small molecules, and macromolecules essential for life. It highlights the significance of elements like carbon, hydrogen, oxygen, and nitrogen in forming biological structures such as carbohydrates, lipids, proteins, and nucleic acids. Additionally, it covers the roles of these macromolecules in energy storage, structural support, and information storage within living organisms.

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Luân Đinh Tiến
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16 views4 pages

Chapter 2 - The Chemicals Components of The Cells

The document discusses the chemical components of cells, focusing on the types of chemical bonds, small molecules, and macromolecules essential for life. It highlights the significance of elements like carbon, hydrogen, oxygen, and nitrogen in forming biological structures such as carbohydrates, lipids, proteins, and nucleic acids. Additionally, it covers the roles of these macromolecules in energy storage, structural support, and information storage within living organisms.

Uploaded by

Luân Đinh Tiến
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© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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THE CHEMICALS COMPONENTS OF THE CELLS

VOCABULARY:
Subatomic: Hạ nguyên tử
Covalent Bond: Liên kết cộng hóa trị
Backbone: Xương sống
Denaturation: Biến tính
I. Chemical bonds:
- Matter is made of combinations of elements
- The smallest particle of an element that still retains its distinctive chemical
properties is an atom
- The characteristics of substances other than pure elements— including the
materials from which living cells are made— depend on which atoms they
contain and the way these atoms are linked together in groups to form
molecules
 To understand living organisms: Crucial to know the chemical bonds
that hold atoms together in molecules are formed
The mass neutrons = The mass as protons, if there are too many or too few,
the nucleus may disintegrate by radioactive decay—but they do not alter
the chemical properties of the atom.
- The Outermost Electrons Determine How Atoms Interact: 2 types of
chemical bonds:
o Covalent Bonds: Strong forces form a covalent bond when two
atoms share one pair of electrons or multiple pairs of electrons.
Electrons may be shared equally or unequally in Covalent Bond:
 The extent of an atom’s ability to attract an electronic called
its electronegativity
 Non-polar: The bonding electrons are share equally between
the 2 atoms
 Polar: bonded atoms have different electronegativities 
unequal sharing of the electrons
o Noncovalent Bonds – Ionic interactions:
Ionic Bonds form by the Gain and Loss of Electrons:
Result from the attraction of a positively charged ion-a-cation-for a
negatively charged ion-an anion.
o Noncovalent Bonds – Hydrogen Bonds: The interaction of a partially
positively charged hydrogen atom in a molecular dipole with
unpaired electrons from another atom, either in the same or different
molecule
o Noncovalent Bonds – Van der Waals interactions: When any two
atoms approach each other closely they create a weak, nonspecific
attractive force called a Van der Waals interaction
o Noncovalent Bonds – Hydrophobic interactions
II. Small molecules in cells:
92 elements occurring naturally in nature: 25 elements are needed to build
living organisms
- Main element (CHON): the most frequently found elements in cells,
forming about 96% of the human body mass
- Trace-elements are the elements are found in small quantity in cells but are
important in biological processes.
Carbohydrates: The simples sugars – the monosaccharides – are compounds
with the general formula (CH2O)n, where n is usually 3,4,5 or 6
Sugars and the larger molecules made from them, are also called
carbohydrates
Water expelled: condensation (trùng ngưng)
Water consumed: hydrolysis (thủy phân)
Liên kết giữa các đường: glycosidic bond

Polysaccharides: Polymer of simple sugars


- Homogeneous polymers: contain only one kind of sugar/ considered to be
“noninformational”
- Heterogeneous polymers: contain 8-10 types of sugars
Glycogen – in humans and animals
Starch and cellulose – in plants
Functions:
 Energy sources:
o Glucose – key energy source for cells  in a series of reactions is
broken down to smaller molecules to release the energy - cells use
simple polysaccharides
o composed only of glucose units → glycogen (animal cells) and
starch (plant cells)
 Structure support:
- cellulose – glucose polysaccharide (the most abundant organic
chemical on Earth)
- chitin – linear polymer of N-acetylglucosamine insect exoskeletons
and fungal cell walls
 Molecular markers:
- glycoproteins and glycolipids of the cell membrane → selective
recognition by other cells, help cells adhere to one another, Blood
type...
Lipids: meaning fat (in Greek word lipos)
- They are non-polar; not soluble in water; soluble in non-polar solvents
(chloroform)
- 2 structural parts: hydrophilic head and hydrophobic tail
 Energy source: Stored in the cytoplasm of many cells in the form of
droplets of triacylglycerol molecules; animal fats; plant oils
 Construction of biological membranes: Phospholipids, Glycolipids,
Cholesterol.
Proteins – Amino acids:
- all have carboxylic acid group (COOH) and amino group (NH2) both
linked to a single C-atom
- differing only in their side chains compose proteins: amino group, carboxyl
group, side chain
- Amino acids linked together  peptide bond
- Polypeptide or protein  two chemically distinct ends: -NH2, -COOH
Special amino acids: Cysteine, Glycine (the smallest amino acid, has a
single hydrogen atom, small size allows it to fit into tight space), Proline
Hierarchical Structure of Protein:
1. Primary structure: the linear sequence of amino acids linked together
by peptide bonds.
2. Secondary structure: folding of the polypeptide chain into local alpha
helices or Beta sheets
3. Tertiary structure: 2nd structure with various loop and turns in a
single polypeptide chain pack into a larger independently stable
structure.
4. Quaternary structure: some individual polypeptide with their own
tertiary structures can associate into a quaternary structure – multichain
complex ( > 2 chains)
Denaturation and Protein folding:
- Regulation: control pr activity
- Structure: tubulin – microtubules, histones – chromosomes
- Signaling: monitoring of the environment and transmitting resultant
information
- Transport: flow of small molecules and ions across membrane
- Catalysis: enzymes
- Motor proteins: generation of force for movement
Enzyme: speed up metabolism, or the chemical reactions in our bodies and
don’t chemically changed at the end of the reaction (Name = substrate + ase)
Characteristics:
- A small amount is needed to catalyze a lot of substrate.
- Specific – each class of enzymes will catalyse only one particular reaction.
- Enzymes catalyse reversible reactions
- Many enzymes are only able to work with in presence of a coenzymes
- Effected by changes in temperature and pH.
Bases:
Pyrimidines: all derive from six-membered pyrimidine ring: cytosine (C), thymine (T),
uracil (U)
Purine: have a second, five membered ring fused to the six-membered ring: adenine
(A), guanine (G)
The most important role  storage of biological information
Two types of nucleic acids:
RNA – ribose + A, G,C i U; mostly single-standed
DNA – deoxyribose + A, G,C i T; double stranded helix
Adenosine triphosphate (ATP)
III. Macromolecules in cells:

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