Republic of the Philippines

Department of Education
MIMAROPA Region
SCHOOLS DIVISION OF PALAWAN
PULOT NATIONAL HIGH SCHOOL
PULOT CENTER, SOFRONIO ESPAÑOLA, PALAWAN

Name:_______________________________ Date:_______________
Grade Level & Section: ________________ Score:______________

WORKSHEET in Science 10 for Fourth Quarter (April 15-16, 2024) IOMOLECULES

PROTEINS-are made up of the elements carbon, hydrogen, oxygen, nitrogen, and sulphur. They are the second most
common molecules found in the human body (after water) and make up about 10% to 20% of the mass of a cell.
Proteins can be classified into two major types-fibrous proteins (e,g. collagen, actin, and keratin), which are insoluble in
water and are the main components of the body; and globular proteins (e.g., albumin, hemoglobin, and immonuglobuline) ,
which are soluble from water and are used for the other non-structural purposes of proteins.
AMINO ACIDS- are organic compounds that contain an amino group and a carboxyl group. Amino acids are the building
blocks of proteins. Of the 20 amino acids found in human protein, only 11 can be synthesized by the body and 9 have to be
supplied by the foods we eat. These 9 amino acids are called essential amino acids. Adults only need 8 of them: valine,
isoleucine, leucine, lysine, methionine, phenylalanine, threonine, and tryptophan. The 9th amino acid-histidine-is only
essential for infants.
A human body has about 100 000 different proteins that help carry out all the bodily functions, which involve the following:
1.Structure. Proteins comprise our skin, bones, hair, and nails. Collagen and keratin are the main structural component in
animals and the two most important structural proteins.
2. Hormones. Many hormones, including insulin, are actually proteins. Insulin helps cells absorb glucose from the blood and
prevents the body from using fat as a source of energy.
3. Transport. Hemoglobin in the blood is an example of transport protein. During cellular respiration, it carries oxygen from
the lungs to the cells, where it is used. Then, haemoglobin carries the resulting carbon dioxide to the lungs for expulsion
outside the body.
4. Storage. Some proteins store materials in the same way that starch and glycogen store energy. Casein in milk store
nutrients for new-born mammals, as does ovalbumin in eggs for birds. Ferritin, a blood cell protein in the liver, stores iron.
5. Catalysis. Enzymes are proteins that speed up all of the reactions that take place in organisms.
6. Protection. When an antigen, a protein from an outside source or some other foreign substance, enters the body, the
body develops its own proteinaceous antibodies to counteract the alien protein and fight disease. Fibrinogen is a protein that
facilitates blood clotting. Without fibrinogen, our wounds will never heal.
7. Movement. The protein molecules in our muscles, myosin and actin, are involved in muscle contraction and relaxation.
8. Regulation. Some proteins not only control and regulate the kind of proteins synthesized in a particular cell but also
dictate the time this should occur.

LEVELS OF PROTEINS STRUCTURE

1.Primary Structure-refers to the arrangement or order of amino acids in the protein chain. When two amino acids combine
through a condensation reaction, a dipeptide is produced. The condensation reaction eliminates water and forms a
covalent bond, a peptide bond, which consists of the carboxyl group of one amino acid and the amino group of another. The
term peptide refers to the two or more amino acid monomers linked by peptide bonds. Peptides that have more than 10
amino acids are called polypeptides, which are produced as more amino acids monomer units are added to the peptide via
multiple condensation reaction.
2. Secondary Structure- refers to the molecular shape caused by hydrogen bonding between the – C=O and –N- N groups
within the chain. The secondary structures are held together by hydrogen bonds. The alpha (α)-helix structure is an example
of a secondary structures of proteins wherein the polypeptide chain forms a spiral configuration. The “alpha” means that if
one looks down the length of the spiral, the coiling happens in a clockwise direction.
3. Tertiary Structure- the interactions primarily between the R groups fold and bend the polypeptide chain. The tertiary
structure is a description of the way chain folds itself in its three-dimensional shape.
4. Quaternary Structure – is the arrangement of two or more interacting polypeptide chains, resulting in the protein
classification fibrous, globular, or conjugated.

DENATURATION OF PROTEIN
It involves the disruption and possible destruction of the secondary and tertiary structures of a protein. It renders the
protein biologically inactive and less folded. Denaturation is not strong enough to break the peptide bonds in proteins,
hence, the primary structure remains the same after the process.
Protein denaturation can be caused by several factors, including pH changes, increase in temperature, and addition of
various chemicals.
KWASHIORKOR- is protein malnutrition which affects children in underdeveloped countries.

NUCLEIC ACIDS- are large biomolecules that include the deoxyribonucleic acid (DNA) and ribonucleic acid (RNA). These
are made from monomers known as nucleotides, which are linked in a chain through condensation reactions.
DNA –serves as information-carrying molecules in biological systems. Some RNA molecules serve as catalyst. DNA and
RNA are involved in the synthesis of the different proteins used by the cell.

NUCLEOTIDES- is formed by combining sugar, base, and phosphate through a series of condensation reactions.

DIFFERENCES BETWEEN THE TWO KINDS OF NUCLEIC ACIDS

DNA(Deoxyribonucleic Acid) RNA (Ribonucleic Acid)

Description It contains the genetic instruction used in It is responsible for the template in the
the development and functioning of all synthesis of proteins which in turn control
living organisms the operation & function of the cell.
Function Long-term storage and transmission of Transfer the genetic information for the
genetic information. creation of proteins from the nucleus to the
ribosomes.
Sugar and Bases Sugar: Deoxyribose Sugar: Ribose
Phosphate-backbone Phosphate-backbone
Four bases: adenine, guanine, cytosine, Four bases: adenine, guanine, cytosine,
thymine uracil
Pairing of Bases A-T (Adenine – Thymine) A-U (Adenine-Uracil)
G-C ( Guanine - Cytosine G-C ( Guanine - Cytosine
Strand Double strand Single Strand

DNA Replication – the DNA in the parent cell must be duplicated prior to cell division so after the process, each new cell
contains the normal amount of DNA material.
The process of DNA replication in all living organisms is the basis for biological inheritance. Furthermore, DNA contains
the genetic information from which the proteins of cells are synthesized. The proteins consequently help facilitate the
activities of organisms.

ACTIVITY: Fill in the complementary DNA strand using DNA base pairing rules.
C A T G T A G G T A A C C T
__ __ __ __ __ __ __ __ __ __ __ __ __ __

ASSESSMENT:
Direction: Write the letter of the correct answer on the space provided before each item.(2pts each)
____1. Amino acids are the building block of __________________.
A. carbohydrates B. lipids C. nucleic acids D. proteins
____2. Amino acid monomers are linked into peptides through ___________________.
A. condensation reaction B. denaturation C. hydrogenation D. hydrolysis
____3. Essential amino acids are __________________.
A. amino acids found in all organisms
B. amino acids essential to make other amino acids
C. amino acids that the body need in order to function
D. amino acids that the body cannot make and must obtained from diet
____4. All of the following make up a nucleotide EXCEPT _____________.
A.carboxyl group B. nitrogen-containing base C. sugar D. phosphate
____5. In DNA , adenine forms a complementary pair with ______________.
A.cytosine B. guanine C. thymine D. uracil
____6. Which nitrogen base is NOT found in ribonucleic acid?
A. adenine B. cytosine C. thymine D. uracil
____7. Which structure of protein results from the arrangement of two or more interacting polypeptide chains?
A.primary structure B. secondary structure C. tertiary structure D. quaternary structure
____8. The following are called essential amino acids EXCEPT ___________.
A. alanine B. phenylalanine C. threonine D. valine
____9. The sugar in RNA is _______________, the sugar in DNA is ________________.
A.deoxyribose, ribose B. ribose, deoxyribose C. ribose, uracil D. ribose, phosphate
____10. Which of the following elements is NOT present in proteins?
A. carbon B. oxygen C. nitrogen D. iron

Prepared by: Checked by:

RUBY S. FABRIGAS CYRUS T. TRIŇO

Science 10 Teacher HTIII/Science Department Head

Noted by:

EDGARDO C. MUTIA
SS Principal III