The University of Jordan

Accreditation & Quality Assurance Center

Course Syllabus

Course Name:
 The University of Jordan Course Syllabus Accreditation and Quality Assurance Center

1 Course title Biochemistry for Nursing

2 Course number 501104

Credit hours (theory, practical) 3
3
Contact hours (theory, practical) 3
4 Prerequisites/corequisites General chemistry

5 Program title Nursing

6 Program code
7 Awarding institution The University of Jordan

8 Faculty Medicine

9 Department Physiology and Biochemistry

10 Level of course Second level

11 Year of study and semester (s) Second year and above (all semesters)

12 Final Qualification
Other department (s) involved in
13
teaching the course
14 Language of Instruction English
15 Date of production/revision December 2018/2019

16. Course Coordinator:

Office numbers, office hours, phone numbers, and email addresses should be listed.
Dr. Mamoun Ahram
School of Medicine, First floor
962-6-535-5000 (ext. 23481)
[email protected], [email protected]
17. Other instructors:
Office numbers, office hours, phone numbers, and email addresses should be listed.
Faisal Al-Khateeb
Said Ismail
Nafez Abu Tarboush
Diala Abu Hassan
18. Course Description:

As stated in the approved study plan.

This three-credit hour course is mandatory for nursing students. The course is designed to introduce nursing
students to biochemistry via reviewing general and organic chemistry, covering the basic concepts of
structures and functions of macromolecules, discussing basic information of enzymes including their
mechanisms of action and regulation, the critical cofactor critical for enzyme function, and their use in the
clinic, describing major metabolic pathways, and presenting main concepts of molecular biology and its
technologies.

19. Course aims and outcomes:

A- Aims:
The overall objective is to learn: 1) the structure of macromolecules and their building block, 2) enzyme function
and their role in metabolism, and 3) concepts of molecular biology and uses of its technologies in the clinic.
B- Intended Learning Outcomes (ILOs): Upon successful completion of this course students will be able to …
A. Knowledge and Understanding: Student is expected to:
A1- List common and most critical elements in the human body.

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The University of Jordan Course Syllabus Accreditation and Quality Assurance Center

A2- Differentiate the types and characteristics of non-covalent interactions.

A3- Know biochemical importance and properties of carbon and water.
A4- Recall the concepts of acids, bases, and amphoteric molecules, and ionization of water and
weak acids.
A5- Apply the molecular expressions: molarity, normality, equivalence, pH, and pKa.
A6- Know the chemical concept of different types of buffers, buffering capacity, midpoint, and
titration.
A7- Apply the Henderson-Hasselbalch equation.
A8- List of physiological buffers and translate knowledge in normal and abnormal condition.
A9- List major functional groups of organic compounds.
A10- Recall the chemical and physical properties and structures of the major functional groups of
organic compounds.
A11- Know the main reactions involving the major functional groups of organic compounds.
A12- Know the concepts macromolecules of and how they are synthesized and broken down.
A13- Define carbohydrates.
A14- Recognize the classifications, drawing, structure, and function of carbohydrates (mono-, di-,
oligo-, and poly-).
A15- Apply the concept of isomerism to monosaccharides.
A16- Identify substituted and modified saccharides (mono- and poly-).
A17- Differentiate proteoglycans and glycoproteins.
A18- Link carbohydrates to blood typing.
A19- Define lipids.
A20- Identify the classifications, drawing, structure, and function of lipids (fatty acids,
triglycerides, waxes, phiospholipids, glycolipids, and steroids.
A21- Differentiate the basic mechanism and players of lipid transport in blood.
A22- Recall the complex structure of cell membranes and the function of the different
components.
A23- Define proteins.
A24- List amino acids.
A25- Differentiate the structure, isomerism, classes of amino acids.
A26- Identify the ionization states of amino acids.
A27- Know the concept of isoelectric point.
A28- List modified and specialized amino acids.
A29- Recall the four levels of protein structure.
A30- Recall of features of peptide bond.
A31- Apply the concept isoelectric point of amino acids to polypeptides \.
A32- Differentiate the different secondary structures of proteins and their structural significance.
A33- Understand the formation of tertiary structure of proteins.
A34- Define quaternary structure.
A35- Know the concept of complex protein structures (glycoproteins, lipoproteins,
phosphoproteins).
A36- Apply the concepts of denaturation and renaturation to protein structure and function.
A37- Apply the previous information to pathological defects in protein formation.
A38- Recognize the different classes of proteins (fibrous, globular).
A39- Discuss different proteins from each class I (mainly collagen, myoglobin, and hemoglobin)
in connection to their function in light of previous knowledge.
A40- Define enzymes.
A41- Recall the general properties and functions of enzymes.
A42- List the classes of enzymes and differentiate the reactions they catalyze.
A43- Recall the major features of active sites.

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The University of Jordan Course Syllabus Accreditation and Quality Assurance Center

A44- Recall the concept of free energy and activation energy.

A45- Define enzyme kinetics.
A46- Apply the concept of Vo, Vmax, and KM, and their biological significance.
A47- Link the mechanisms of action of the different classes of inhibitors .
A48- Know the role of the factor of diffusion (compartmentalization and enzyme complexing) in
enzyme regulation.
A49- Describe how enzyme activity can be regulated by physiological and pharmacological
inhibitors.
A50- Recall the concept of allosteric regulation.
A51- Identify the role of enzyme regulatory molecules.
A52- Comprehend the mechanisms of reversible and irreversible enzyme modification.
A53- Define modes of regulation.
A54- Discuss the effect of nonspecific inhibitors (temperature, pH) on protein structure and
function.
A55- Define isoenzymes and know their biological and clinical significance.
A56- Identify the role of enzymes in clinical medicine.
A57- Differentiate between holoproteins and apoproteins.
A58- Differentiate classes of cofactors including vitamins.
A59- Define and list vitamins and understands their contribution in enzymatic reaction .
A60- Identify the role of metals in enzyme activity of metal-activate enzymes.
A61- Recall the means of generating biochemical energy through:.
a. Citric acid cycle.
b. Oxidative phosphorylation.
c. Respiratory chain reaction.
A62- Recall the major metabolic pathways of carbohydrates including:.
a. Glycolysis.
b. Fate of pyruvate.
c. Glycogenesis.
d. Glycogenolysis.
e. Gluconeogenesis.
A63- Identify the role of the different pathways in feeding, starvation, and fasting.
A64- Recall the major metabolic pathways of lipids (fatty acid synthesis and beta-oxidation of
fatty acids).
A65- Recall the major metabolic pathways amino acids including urea cycle.
A66- Define nucleic acids and nucleotides.
A67- Identify the classifications, drawing, structure, and function of nucleic acids.
A68- Recognize the mechanism of DNA and RNA structure and synthesis and their physical
properties.
A69- Explain the higher organization of DNA into chromosomes.
A70- Comprehend the mechanism of DNA replication.
A71- Recall the different major RNA molecules.
A72- Know the processes of transcription and translation in prokaryotes and eukaryotes.
A73- Get oriented of recombinant DNA technologies their use in diagnostics.

B. Intellectual Analytical and Cognitive Skills: Student is expected to

B1- Calculate pH and changes in pH according to different variables.
B2- Predict changes in blood pH according to equilibrium of bicarbonate buffering system.
B3- Link the main features, structures, and chemical reactions of discussed functional groups of
organic compounds with the studied macromolecules.
B4- Differentiate between the various sugar molecules, lipids, and amino acids.
B5- Determine enzyme class according to catalyzed reaction and involved cofactor.

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The University of Jordan Course Syllabus Accreditation and Quality Assurance Center

B6- Interpret basic data of recombinant DNA technologies.

20. Topic Outline and Schedule:

Evaluation
Topic Week Instructor Achieved ILOs Reference
Methods
Introduction, 1 TBD A1-3 12 (325-326)
intermolecular 5 (99-105; 117-
forces, carbon, 121)
water 8 (209-214)
Acid and 1 TBD A4-8
bases, pH,
10
buffers,
titration
Introduction 2 TBD A9-11
to organic
chemistry:
structure,
properties &
important
reactions of
hydrocarbons, 12-17
alcohols,
phenols,
ethers,
aldhyds,
ketones,
carboxylic
acids & amines
Carbohydrate 3 TBD A12-18
s: structures,
22
classes,
function
Lipids: 4 TBD A19-22
structure &
classification,
Fatty acids,
Triglycerides, 24
phospholipids,
Glycolipids &
cholesterol,
cell membrane
Amino acids 5 TBD A23-39
and proteins:
amino acids,
protein 18
structure,
properties of
proteins
Enzymes: 6 TBD A40-A56
general
properties of
enzymes,
classes, the
19
effect of
substrate &
enzyme
concentration
on reaction

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The University of Jordan Course Syllabus Accreditation and Quality Assurance Center

rate, enzyme
inhibition &
regulation of
enzyme
activity,
enzymes in
medicine
Vitamins 7 TBD A57-A60
vitamins,
minerals & 19
trace elements
in nutrition
Generation of 7,8 TBD A61
Biochemical
Energy: citric
21
acid cycle &
respiratory
chain
Carbohydrate 9 TBD A62-A63
Metabolism:
digestion,
glucose
23
metabolism,
glycolysis,
glyconegenesi
s
Lipids 10 TBD A64
Metabolism:
digestion,
absorption,
transport,
oxidation & 25
biosynthesis of
fatty acids,
biosynthesis of
cholesterol,
ketoacidosis
Protein and 11 TBD A65
amino acid
Metabolism:
catabolism & of
amino acids,
urea cycles, 28
amino acids
conversion,
synthesis of
amino acids
catabolism
Nucleic acid 12 TBD A66-72
and protein
synthesis:
heredity & the
cell, structure 26
of nucleic
acids, RNA,
genetic code
translation
Genomics 13 TBD A73
Mapping 27
human

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 The University of Jordan Course Syllabus Accreditation and Quality Assurance Center

genome,
chromosomes

21. Teaching Methods and Assignments:

Development of ILOs is promoted through the following teaching and learning methods:

Lectures (1005)

22. Evaluation Methods and Course Requirements:

Opportunities to demonstrate achievement of the ILOs are provided through the following assessment methods
and requirements:
Exam I: 30%
Quiz: 20%
Final exam: 50%
23. Course Policies:

Attendance policies:
Attendance is mandatory
B- Absences from exams and handing in assignments on time:

Make-up exam is given if absence is accepted by the deanship

C- Health and safety procedures:

None
D- Honesty policy regarding cheating, plagiarism, misbehavior:

Misbehavior is not permitted and is subjected to punishment according to university laws and
regulations
E- Grading policy:

Exams are scored electronically

F- Available university services that support achievement in the course:

Lecture halls, computers, and datashows are provided

24. Required equipment:

Computers and datashows

25. References:
A- Required book (s), assigned reading and audio-visuals:

Fundamentals of General, Organic & Biological Chemistry 5th Edition, by John

McMurry & M.E.Castellion

B- Recommended books, materials, and media:

26. Additional information: