Questions

in
Cell Biolog
(1)………….is
CELL the fundamental unit of life
(2)The concept that the cell is the basic unit of
life is known as the…………….
CELL THEORY
Prokaryotic
(3)………………..cells lack a nuclear envelope,
while… ………….. have a nuclear membrane
Eukaryotic
(4) Compound that can dissolve in water
called…………Hydrophilic
(5) Molecules that have both hydrophobic and
hydrophilic ends are said to be …………..
Amphipathic
(6)The formation of large biological molecules
from smaller building blocks releases
…………
WATE
(7)RA cell makes a large number of polymers
from a small group of…………..
MONOMER
(8) Proteins are made from only 20 different
Amino
……….…, while, DNA is built from four
Acid Nucleotides
kinds of………..
 Complex lipid
(9)…………..……..simple lipids that contain
additional elements such as phosphorus, nitrogen,
sulfur, or small hydrophilic organic compounds

(10)……………..is
Fatty Acids commonly used as a building
block of more structurally complex lipids

Cholesterol a steroid that plays a significant

(11)……………….Is
role in the structure of the cell membrane and
from which we synthesize sex hormones and
vitamin D2
(12) Lipids in water can generate three most
Liposome …….
common configurations ………….…..,
……., …………..
Micelle Bilayer sheet
Monosaccharide
(12)Sugar monomers are……………….….,
such as glucose, mannose and fructose
Starch
(13)Plants store …………..as energy storage,
Glycogen
while animals store……………..
(14) Monosaccharide that have five carbon
atoms are called…………..
Pentoses
 Oligosaccharide
(15)…………………….carbohydrates
containing several monosaccharides

Chitin
(16)……………Is a polysaccharide used by
insects and crustaceans to build an exoskeleton

(7)………………..is
Cellulose a polymer of glucose that
forms plant cell walls
 Short polymer Unlinked
monomer
Dehydration
)1(

Polymer
(2) Liposome
)4(
Micelle
)5(

Hydrolysis
(3) )6(

Bilayer sheet
 Protein
-Are polymer built from 20 different amino acid (monomers)

- Are the most abundant macromolecules in cells

-Represent more than 50% of the dry mass of cells

-Have an important structural and enzymatic roles

-Transmit information (messages) between cells (protein

hormones)
 Protein
- Proteins embedded in the plasma membrane form
channels that control the passage of small
molecules into and out of the cell
- Provide a defense against infection (antibodies)
-Transport and store other molecules such as
oxygen
- Generate movement
- Transmit nerve impulses
- Control growth and differentiation
 Protein function
Proteins divided into two groups based on its function in the cells:

Structural proteins: Integral parts of cellular structures (Fibrous

proteins (Collagen) , cartilage, skin and bone (keratin(, tubulin,
actin like proteins, microtubules and, Microfilaments

Dynamic proteins :Catalytic proteins; catalysts for chemical

reactions, cell metabolism (hormones , insulin, erthrprotein
and thyroxine, hemoglobin-hemocyanin-myoglobin
 Protein
Proteins can be divided into three main classes according to
its tertiary structures:
1- Globular proteins: or spheroproteins, all are soluble
and many are enzymes.
2- Fibrous proteins: or Scleroproteins, they are often
structural, such as collagen (connective tissue), or keratin
(skin, hair and nails)
3- Membrane proteins: Membrane proteins often serve
as receptors or provide channels for polar or charged
molecules to pass through the cell membrane.
 Amino Acids
Most consist of carbon, hydrogen, oxygen, and nitrogen; 2
contain sulfur, 1 contains selenium
All contain two important functional groups:
Carboxylic acid group (-COOH)
Amino group (-NH2)
The side chain is the most important in determining its
contribution to protein structure and activity
 Peptide bond
• Amino acid monomers held together by covalent
bonds (peptide bonds)
• This bond links the carboxyl group of one amino acid
to the amino group of the next amino acid
Polypeptides: thousands or millions of amino acids
Have two distinct ends:
Amino group (the amino- or N- terminus)
Carboxylic group (carboxyl or C-terminus)
Protein consists of a specific amino acid sequence
The amino acid sequence of protein determines its three
dimensional structure and its chemical reactivity.
 Conjugated proteins
A conjugated protein is a protein that functions in
interaction with other chemical groups
Nucleoproteins: chromosome
Chromoprotein: haemoglobin
Phosphproteins: found in milk
Glycoproteins : contain oligosaccharide chains
covalently attached to their polypeptide side-
chains, they play a role in cell-cell interactions
Lipioproteins: enzymes, transporters
 Levels of protein structure
• Protein can have four
levels of structure Four Levels of Protein Structure

1- Primary structure Primary structure

Amino acids

2- Secondary structure Hydrogen

bond

3-Tertiary structure Secondary structure

Alpha helix Pleated sheet

4-Quaternary structure
Tertiary structure Polypeptide
(single subunit
of transthyretin)
 Primary structure
Primary structure: sequence of amino acids in a polypeptide
-The correct amino acid sequence is determined by the cell’s
genetic information
-The slightest change in this sequence affects the protein’s ability
to function
-Sickle cell disease is manifested by an inability of hemoglobin
in red blood cells to carry oxygen, the primary function of
hemoglobin.
-This blood disorder is the result of change in a single amino acid
 Secondary structure
• Secondary structure: the regular arrangement of amino acids
within localized regions of the polypeptide
• Folds in polypeptide that form a more stable structure, often
involving hydrogen bonding between R groups
• There are two types of secondary structure:
Helical structure called an alpha helix (α-helix) (region of
polypeptide chain coils around itself
Pleated sheet (β sheet): two parts of polypeptide chain lie side
by side with hydrogen bonds between them.
 Tertiary structure
 Tertiary structure: additional folding of polypeptide to result in
greater stability and unique three-dimensional shape
 Forms exposed regions or grooves in the molecule that are

important for binding other molecules

 Disulfide bonds: bonds between -SH groups from two different

amino acids
 In most proteins combination of alpha helix and beta sheets
connected by loop regions of polypeptide chain, fold into compact
globular structures called Domains (the basic unit of tertially structure)
 Quaternary structure
• Quaternary structure: occurs in proteins composed of two or more
polypeptides
– Subunit: each polypeptide in the protein, held together by
either/both covalent and noncovalent linkages
– Homodimer: protein containing two identical subunits
– Heterodimer: protein containing two nonidentical subunits
 ‫المحاضرة القادمة‬
‫األحماض النووية واألنزيمات‬
‫‪Good Luck‬‬
‫‪Dr Mona‬‬
• The spherical structure is induced by the
protein's tertiary structure. The molecule's
apolar (hydrophobic) amino acids are
bounded towards the molecule's interior
whereas polar (hydrophilic) amino acids are
bound outwards