This document provides an overview of a biochemistry course for nursing students. It outlines the course objectives, which include understanding biomolecules, metabolic processes, gene function, and the scientific basis of disease. The course will be taught through lectures, practical sessions, assignments, and exams. Topics to be covered include amino acids, protein structure, carbohydrate metabolism, lipid metabolism, vitamins, and gene expression. Recommended textbooks are provided, and the lecture schedule lists the weekly topics and assigned readings.

1. Biochemistry
for Nursing Students
CHS 262

2. Biochemistry CHS 262
This course Prepared by
Dr.Eman Saqr
2
Course Directors
***********
Associate Prof. Dr. Ehab(Male)
Assistant Prof.Dr. Eman Saqr (Female)

3. Introduction
This course aims to enhance the study of
general and basics of Biochemistry for nursing
students.
•Biochemistry is the language of biology.
• The tools for research in all the branches of
medical science are mainly biochemical in
nature.

4. The study of biochemistry is essential to
understand:
Biomolecules.
How the food that we eat is digested, absorbed, and used
to make ingredients of the body?
How does the body derive energy for normal day to day
work?
How are the various metabolic processes interrelated?
What is the function of genes?
The study of biochemistry is necessary to give the
scientific basis for disease and is useful for intelligent
treatment of patients.

5. Recommended Books, References &
Teaching Materials
•Biochemistry by P.C. Champe, R.A. Harvey and
D.R. Ferrier 3rd Edition 2005 Lippincott’s
Illustrated Reviews
•Textbook of biochemistry for dental students by
DM Vasudevan, Sreekumari S and Kannan
Vaidyanathan, 2nd Edition 2011.
•Handbook of biochemistry (For allied and
nursing students) by Shivananda Nayak B 1st
Edition 2007.

6. Teaching Methodology:
• Lecture. 2hours
•Practical Session. 2hours
Assessment Tools:
20% Mid term-Exam
20% Assignments
20% Practical
40% Final Exam
Assignments are:
• 5 marks for each of Research project, Oral, and
Quizzes.
• 5 marks for attendance, attitude and participation
during lecture session.

7. Lectures schedule
Week Date/Saturday Subject Reading assignment Quizzes
1 26/1/2013 Registration
2 2/2/2013
Introduction of
biochemistry and
explain the course
syllabus
Amino acids
Biochemistry, 3rd Edition 2005
Lippincott’s Illustrated Reviews
Unit I/ Chapter 1 pp. 1-12
3
9/2/2013
Structure of proteins. Unit I/ Chapter 2 pp. 13-24
4 16/2/2013
Nitrogen metabolism. Unit IV/ Chapter 19 pp. 245-260 Quiz 1
5
23/2/2013 Enzymes. Unit I/ Chapter 5 pp. 53-68
6 2/3/2013
Introduction to
carbohydrates and
Glycolysis
Unit II/ Chapter 7, 8 pp. 83-108 Quiz 2
7
9/3/2013
Mid Term Exam
8
16/3/2013
Tricarboxylic acid cycle
and Gluconeogenesis.
Unit II/ Chapter 9, 10 pp. 109-124
9 23/3/2013 Mid Term Vacation

8. 10 30/3/2013
Glycogen metabolism Unit II/ Chapter 11 pp.
125-136
11 6/4/2013
Metabolism of dietary
lipids
Unit III/ Chapter 15
pp.173-180
12
13/4/2013 Fatty acid and
triacylglycerol
metabolism.
Unit III/ Chapter 16
pp. 181-200
Quiz 3
13
20/4/2013 Water soluble
vitamins
Unit V/ Chapter 27 pp.
373-381
14 27/4/2013
Fat soluble vitamins Unit V/ Chapter 27 pp.
381-394
15 6/5/2013
Gene expression
and protein synthesis
Unit VI/ Chapter 31
pp.431-448
Quiz 4
16
13/5/2013 Practical Exam
17
20/5/2013 Oral Exam
18
27/5/2013
Final Exam
19
1/6/2013
5/6/2013 Summer Vacation

9. Project
• Each one can choose one diseases a
subject of the project.
• Five students from each group will
discuss their project weekly starting from
the third week according to their
presence in the attendance sheet.
• The only excuse is by recommended
medical certificate.

10. Female-TableTime
Course Time
Tuesday
Theoretical 8-10
Class
Practical Tuesday
10-12
Office Hours Tuesday
12-2

11. Male-TableTime
Course Time
Wednesday
Theoretical 6-8
Class
Practical Wednesday
8-10
Office Hours Saturday
7-9

12. Biomolecules
 The human body is composed of 6 elements, oxygen,
carbon, hydrogen, nitrogen, calcium and phosphorus.
 Human body is composed of about 60% water, 15%
proteins, 15% lipids, 2% carbohydrates and 8% minerals.
 Biomolecules are covalently linked to each other to form
macromolecules of the cell, eg. Glucose to glycogen and
amino acids to proteins.
 Major complex biomolecules are proteins,
polysaccharides, lipids and nucleic acids.
 The macromolecules associate with each other to form
supramolecular systems, e.g. ribosomes, lipoproteins.

13. Protein
• Proteins are the most abundant and functionally diverse
molecules in living systems.
• Virtually every life process depends on this class of
molecules. For example, enzymes and polypeptide
hormones direct and regulate metabolism in the body,
whereas contractile proteins in muscle permit movement.
• Proteins are group of organic compounds composed of
carbons, hydrogen, oxygen and nitrogen (sulphur and
phosphorus may also present).
• They are the most important of all biologic substances .
• They are polymers of L-amino acids linked together by
peptide bonds.

14. Amino acids
Although more than 300 amino acids have
been described in nature, only 20 are
commonly found as constituents of
mammalian proteins
• They are the building blocks of proteins.
• They are organic compounds, which contain
two functional groups, amino group (-NH2)
and carboxyl group (-COOH).
• The amino group is usually attached to the α-
carbon atom (next to the -COOH group).

16. • Amino acids present in proteins are of the α-L-type
i.e. the amino (H2N-) group is present on the left
side of the vertical formula.
• At physiologic pH (7.4), the carboxyl group is
dissociated, forming the negatively charged
carboxylate ion (-coo-), and the amino group is
protonated (-NH3
+).
• Thus, it is the nature of the side chains that
ultimately dictates the role an amino acid plays in a
protein.

18. Classification of amino acids
• According to the properties of their side
chains, that is, whether they are:
A. Nonpolar, have an even distribution of
electrons.
B. Polar, have an uneven distribution of
electrons, such as acids and bases.

19. A. Amino acids with nonpolar side chains
• These groups are hydrophobic and lipophilic.
• Each of these amino acids has a nonpolar
side chain that does not gain or lose protons
or participate in hydrogen or ionic bonds.
• As, Glycine, Alanine, Valine, Leucine,
Isoleucine, Phenylalanine, Tryptophan,
Methionine, Proline.
• The side chains of these amino acids can be
thought of as ‘oily’ or lipid-like,

20. Location of nonpolar amino acids in proteins:
• In proteins found in aqueous solutions- a polar
environment- the side chains of the nonpolar amino
acids tend to cluster together in the interior of the
protein.
• The nonpolar R-groups thus fill up the interior of
the folded protein and help give it its three
dimensional shape.
• However, for protein that are located in a
hydrophobic environment, such as a membrane, the
nonpolar R-groups are found on the outside surface
of the protein, interacting with the lipid
environment (F. 1.4).

22. Proline:
• Proline differs from other amino acids in that
proline’s side chain and α-amino N form a rigid,
five-membered ring structure (F 1.5).
• It is frequently referred to as imino acid.
• The unique geometry of proline contributes to the
formation of the fibrous structure of collagen,
and often interrupts the α-helices found in
globular proteins.

23. B. Amino acids with uncharged polar
side chains
• These groups are hydrophilic in nature.
• As, Serine, Threonine, Tyrosine, Asparagine,
glutamine, Cysteine.
• These amino acids have zero net charge at neutral
pH.
• Serine, Threonine and Tyrosine each contain a polar
Hydroxyl group that can precipitated in hydrogen
bond formation.
• The side chain of asparagine and glutamine each
contain a carbonyl group and an amide group, both
of which can also participate in hydrogen bonds.

24. 2. Side chains as sites of attachment
for other compounds:
• Polar hydroxyl group of serine, threonine,
and rarely, tyrosine, can serve as a site of
attachment for structures such as a
phosphate group.
• In addition, the amide group of asparagine,
as well as the hydroxyl group a serine or
threonine, can serve as a site of attachment
for oligosaccharide chains in glycoproteins.

25. C. Amino acids with acidic chains
• These groups are hydrophilic in nature.
• The amino acids aspartic and glutamic acid are
proton donors.
• At physiologic pH, the side chains of these
amino acids are fully ionized, containing a
negatively charged carboxylate group (-COO-).
• They are, therefore, called aspartate or
glutamate to emphasize that these amino acids
are negatively charged at physiologic pH.

27. D. Amino acids with basic side chains
• These groups are hydrophilic in nature.
• The side chains with basic amino acids accept
protons.
• Ex., arginine, lysine, histidine.
• However, when histidine is incorporated into a
protein, its side chain can be either positively
charged or neutral.
• This is an important property of histidine that
contributes to the role it plays in the functioning of
proteins such as hemoglobin.

28. Amino acids with basic chains

29. Abbreviations and symbols for
commonly occurring amino acids
• Each amino acid name has an associated three-letter
abbreviation and a one-letter symbol.
• The one-letter codes are determined by the
following rules:
1. Unique first letter:
If only one amino acid begins with particular letter,
then that letter is used as its symbol.
For example, I = isoleucine.

31. 2. Most commonly occurring amino acids have
priority:
If more than one amino acid begins with a particular
letter, the most common of these amino acids
receives this letter as its symbol.
For example, glycine is more common than
glutamate, so G = glycine.
3. Similar sounding names:
Some one-letter symbol sound like the amino acid
they represent.
For example, F= phenylalanine, or
W = tryptophan

32. 4. Letter close to initial letter:
For the remaining amino acids, a one-letter symbol
is assigned that is as close in the alphabet as possible
to the initial letter of the amino acid, for example,
K= lysine
B is assigned to Asx, signifying either aspartic acid
or asparagine.
Z is assigned to Glx, signifying either glutamic
acid or glutamate.
X is assigned to an unidentified amino acid.

33. Classification according to nutritional
requirement
1- Essential or indispensable:
• These groups are essential for growth.
• Their carbon skeleton of these amino acids
cannot be synthesized by human being.
• These include, Isoleucine, Leucine,
Threonine, Lysine, Methionine,
Phenylalanine, Tryptophan and Valine.

34. 2- Partially essential or semi-essential:
• Growing children require them in food, but they
are not essential for the adult individual.
• These include, Histidine and Arginine.
2- Nonessential or dispensable:
• The remaining 10 amino acids are nonessential.
• They also required for normal protein synthesis.
• Their carbon skeleton can be synthesized by
metabolic pathways.

35. Physical properties of amino acids
Optical properties
• All amino acids except glycine are optically active.
• Each optically active amino acid contains one
asymmetric α-C atom attached to four different
groups.
• They occur in D and L forms.
• The naturally occurring amino acids in proteins are
of the L-α amino acid form.
• D-amino acids are found in some antibiotics and
bacteria.

37. Acidic and basic properties of amino
acids
• Amino acids in aqueous solution contain weakly
acidic α-carboxyl groups and weakly basic α-
amino groups.
• In addition, each of the acidic and basic amino
acids contains an ionizable group in its side chain.
• Thus, both free amino acids and some amino
acids combined in peptide linkages can act as
buffers.

38. B. Buffers
• A buffer is a solution that resist change in pH
following the addition of an acid or base.
• In biochemistry: An ionic compound that
when added to a solution neutralizes both acids
and bases without significantly changing the
original acidity or alkalinity of a solution
• Buffer capacity:
It is the ability of the buffer to resist changes in pH
when an acid or base is added.

39. Acid-Base balance
• Normal pH:
• The pH of plasma is 7.4 in normal life, the variation of
plasma pH is very small. The pH of plasma is maintained
within a narrow range of 7.38 to 7.42. The pH of the
interstitial fluid is generally 0.5 units blow that of the
plasma.
• Acidosis:
• If the pH is blow 7.38, it is called acidosis. Life is
threatened when pH is lowered below 7.25. Death occurs
when pH is below 7.
• Alkalosis:
• When the pH is more than 7.42, it is alkalosis. It is very
dangerous if pH is increased above 7.55. Death occurs
when the pH is above 7.6.