TABLE OF CONTENTS

BASIC BIOCHEMISTRY FOR HEALTH SCIENCES

Content Page

General Information 2

Teaching Faculty Contact Information 3

Course Overview 4

I. Course Description 4

II. Course Main Objectives 4

III. Intended Learning Outcomes 5

IV. Intended Learning Outcomes of Each Session 6

V. General Schedule 11

VI. Course Assessments 13

Make-Up Policy 15

Plagiarism Policy 16

COURSE GENERAL INFORMATION

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Information Details

Course Name Basic Biochemistry for Health Sciences

CourseFaculty
Code &Name Email address
BCHM 211
NumberTitle / Department / Office Room No. Extension No.
Dr. Saad Al Qarni

1 Assistant Professor CHEM 112,BIOL 111

Pre-Requisites
Office Rm No. 159 , Building
alqarnisa@ksau-hs.edu.sa

9
CourseDr.
Format Lecture sessions, Laboratory sessions
Suha Al Thubaiti

2 Assistant Professor
Office Rm No. 159 , Building
Althubaitis@ksau-hs.edu.sa
Number of Credit 99259
4 hrs
Hours
Dr. Nimer Mehyar

3 Assistant Professor
CourseOffice
Duration
Rm No. 159 13, weeks
Building
mehyarn@ksau-hs.edu.sa

9
Dr. Ahmed Aljohani
Course Dates 28 August 2022 – 24 November 2022
4 Assistant Professor
Office Rm No. 159 , Building
johaniah@ksau-hs.edu.sa

Dr. Amal Alsufyani 95655

Course Coordinator
Dr. Mohammed Hamad

5 Professor
Reference Book
Office Rm No.
hamadm@ksau-hs.edu.sa
Lehninger Principles of Biochemistry
7th, edition,
159 Building2017, David Nelson and Michael Cox, Publisher: Macmillan
45500
Dr. Abdulmajeed Al Harbi

6 Assistant Professor
Office Rm No.
harbiabd@ksau-hs.edu.sa
1. Lippincott‘s Illustrated Reviews Biochemistry 7th Edition, Harvey & Ferrier
159 , Building
2017
Other Reference 45526
2. Harpers Biochemistry (30th ed.), 2015, W.H.Freeman
Materials
Dr. Amal Alsufyani
Harper Biochemistry (e-book)
7 Assistant Professor
Office Rm No.
http://www.accessmedicine.com/resourceTOC.aspx?resourceID=18
159 , Building
sufyania@ksau-hs.edu.sa

45649
Dr. Shereen Jamalalddin

8 Assistant Professor
Office Rm No. 159 , Building
Jamaladdins@ksau-hs.edu.sa

45544

TEACHING FACULTY CONTACT INFORMATION

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COURSE OVERVIEW
I. Course Description

This is a one trimester course designed to introduce concepts of biochemistry of

macromolecules, including the structure and function of proteins, nucleic acids, sugars and lipids.
The main concepts related to acid-base and buffers will be taught. The course also introduces the
classification and the types of vitamins and coenzymes and their role in metabolism. The
fundamentals of thermodynamics and the metabolic role of high energy molecules will be
discussed. The fundamental concepts of how receptors regulate cell function through signal
transduction networks will be discussed. The enzymology component of the course is meant to
introduce the main concepts of enzymes’ structure, functions, catalysis, different types of
inhibitors and different modes of enzymes’ regulation. Techniques to study biomolecules like
proteins and their relevance to understanding biology will be illustrated. Six laboratory sessions
will be conducted to illustrate aspects of the theoretical course, and to teach students essential
practical skills.

II. Course Main Objectives

The main objective of this course in to enable the students to:

 Define the chemical structures of cellular macromolecules and nutrients, i.e.

carbohydrates, lipids, nucleic acids & proteins, vitamins and coenzymes.
 Recognize the basis of cellular signaling and transport.

 Understand the mechanism of enzymes, their kinetics, and their role in regulating
cellular functions.

 Describe main concepts of bioenergetics.

III. Intended Learning Outcomes

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Learning Domains and Course Learning Outcomes

1. Knowledge and Understanding
Recognize the structure and function of the macromolecules including carbohydrates, proteins, nucleic
1.1 acids, lipids and vitamins

1.2 Define the main concepts of enzymes’ structures, functions, types of inhibitors and regulation.

1.3 Describe main concepts of bioenergetics.

2. Skills
2.1 Explain the relationship of macromolecules’ structures and functions.

2.2 Discuss the major signaling pathways and their functions.

2.3 Explain enzymes’ kinetics, regulation, inhibition and catalytic mechanisms.

2.4 Perform general biochemical calculations for different unit conversions, finding molar concentrations
and establishing standard curve.
2.5 Perform various practical biochemical techniques in the laboratory such as micro-pipetting and buffer
preparation.

3. Values
3.1 Form work groups, distribute tasks, and lead group discussion.

IV.Intended Learning Outcomes of Each Session:

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IV .1. Lectures
Session 1 Title: Introduction to Biological Molecules

At the end of this lecture, students should be able to:

 Recognize features of living organisms

 Explain the central role of carbon atom in biomolecules
 Summarize the main types of macromolecules
 Explain the importance of 3D structure of macromolecules

Session 2 & 3 Title: Water & Buffers

At the end of this lecture, students should be able to:

 Explain the importance of water as a universal solvent

 Recognize water structure and describe hydrogen bonding
 Describe water interactions with biological molecules.
 Explain osmosis in respect to water
 Explain (briefly) water ionization constant, pH scale, weak acids and bases dissociation constants and
buffering systems

Session 4 & 5 Title: Amino Acids and Polypeptides I & II

At the end of this lecture, students should be able to:

 Describe the structures of 20 amino acids and three letter nomenclature system.
 Classify amino acids according to their chemical properties
 Recognize some of the uncommon amino acids and their functions
 Explain amino acids action as buffers and explain their characteristic titration curves.
 Explain the formation of peptide bonds and amino acids polymers

Session 6 - 8 Title: Protein Primary, Secondary and Tertiary Structures I, II and III

At the end of this lecture, students should be able to:

 Explain how protein structure is determined by primary structure and peptide bond structural and
chemical properties
 Define protein secondary structure and identify the structural properties of the most common
conformations including -helix, -sheets and -turns.
 Define protein tertiary structure and its structural organization.
 Define quaternary structure and its structural organization
 Describe briefly protein folding
 Explain assisted protein folding and describe chaperons function

Session 9 & 10 Title: Working With Proteins I & II

At the end of this lecture, students should be able to:

 Describe methods of separation and purification

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 Describe crude extract preparation, differential centrifugation.

 Describe fractionation by chromatography.
 Describe protein separation by SDS-PAGE and isoelecric focusing.
 Describe quantification of protein

Session 11 - 12 Title: Protein Function – Hemoglobin I&II

At the end of this lecture, students should be able to:

 Describe myoglobin as an example of globular protein

 Compare myoglobin and hemoglobin
 Explain oxygen binding to heme prosthetic group.
 Compare O2 and CO binding to heme group
 Explain hemoglobin transport of oxygen (taut and relaxed structures)
 Explain 2,3-bisphosphoglycerate regulation of oxygen binding to hemoglobin

Session 13 Title: Protein Function – Actin and Myosin

At the end of this lecture, students should be able to:

 Describe briefly muscle contraction
 Describe myosin and actin structures
 Describe control proteins (tropomyosin and troponin)
 Outline the role of calcium in muscle contraction

Session 14 - 16 Title: Biosignaling I, II & III

At the end of this lecture, students should be able to:

 Describe types of signaling systems in living cells

 Define signal transduction and explain its properties
 Describe structure and function of G-protein coupled receptors: types, ligand binding, amplification,
inactivation, termination and desensitization,
 Explain the functions of different second messengers cAMP, IP3 and Ca2+
 Describe structure and function of enzyme-linked receptors
 Explain insulin receptors function, insulin binding, insulin signal transduction pathways
 Describe types of ion gated channels and their role in nerve signaling

Session 17 Title: Vitamins & Coenzymes

At the end of this lecture, students should be able to:

 List vitamins types and classification

 Describe the structure and biological function of lipid soluble vitamins: A,K,E and D
 Describe the structure and biological functions of water soluble vitamins: C and B complex and
derived coenzymes
 List coenzymes types and classification
Session 18 Title: Bioenergetics I: Thermodynamics

At the end of this lecture, students should be able to:

 Define the two laws of thermodynamics

 Describe the relationship between thermodynamics and bioenergetics

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 Briefly explain thermodynamics parameters (G, H, S)

 Explain the difference between G and G°
 Explain the concept of coupling favourable to unfavourable processes

Session 19 Title: Bioenergetics II: High Energy Molecules

At the end of this lecture, students should be able to:

 Explain how the energy of ATP hydrolysis and phosphoryl group is used to drive biological reactions
 Explain ATP advantages as energy source
 Explain the role and action of other important high energy molecules
 Explain how electron flow through biological oxidization-reduction reactions can be used to drive
biological reactions
 Explain the role of universal electron carriers in biological oxidation-reduction reactions

Session 20 Title: Enzymes I: Structure and Function

At the end of this lecture, students should be able to:

 Define enzymes as reaction catalysts

 Classify enzymes according to international classification
 Define and differentiate between cosubstartes, coenzymes and prosthetic groups
 Explain pH and temperature effects on enzyme activity

Session 21 Title: Enzymes II: Catalysis

At the end of this lecture, students should be able to:

 Explain proximity model and enzyme-substrate complex formation.

 Explain transition state stabilization and lowering of activation energy
 Describe different catalysis mechanisms including: acid-base, covalent, metal and electrostatic
mechanisms
 Describe chymotrypsin catalysis mechanism

Session 22 Title: Enzymes III: Kinetics and Inhibition

At the end of this lecture, students should be able to:

 Explain how kinetic measurements are performed

 Explain the effect of substrate concentration on enzyme activity and ES complex formation
 Briefly describe Michaelis-Menten equation derivation and explain its parameters (Vmax, V
½max, Km) and their limitations
 Identify and explain types of inhibition
 Explain pH and temperature effects on enzyme activity

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Session 23 & 24 Title: ENZYMES IV: REGULATION

At the end of this lecture, students should be able to:

 Define regulatory enzymes

 Explain allosteric enzymes and allosteric regulation
 Explain the effect of homotropic and heterotopic regulators
 Explain enzyme regulation by reversible covalent modification
 Explain enzyme regulation by proteolytic cleavage

Session 25 & 26 Title: Carbohydrates Structure and Functions I & II

At the end of this lecture, students should be able to:

 Describe general structures of monosaccharides

 Compare aldoses to ketoses
 List and compare different types of isomers in monosacharides
 Describe structures and properties of disaccharides
 Recognize reducing sugars from nonreducing sugars
 Describe and compare structure and biological function of major polysaccharides (starch, glycogen
and cellulose)
 Explain (briefly) the types of glycoconjugates

Session 27 & 28 Title: Lipid Structure and Function I & II

At the end of this lecture, students should be able to:

 Describe the biological roles of lipids

 Describe storage lipids structure and properties
 Describe membrane lipids structure and properties
 Describe signaling lipids structure and properties

Session 29 & 30 Title: Nucleic Acids Structure and Function I & II

At the end of this lecture, students should be able to:

 Describe the biological function of nucleotides and nucleic acids

 Recognize the structures of common nucleotides
 Describe the structure of double-stranded DNA
 Describe the structures of ribonucleic acids

IV.2. Laboratory

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Laboratory Session 1-2 Title: Buffers, PH and molar calculation

At the end of this lecture, students should be able to:

 Prepare stock solutions with different molarities.
 Perform pH measurement and buffer preparation
 Understand the concept of ‘pH’
 Prepare phosphate buffer following the given protocol

Laboratory Session 3-4 Title: Protein assay and calibration curve

At the end of this lecture, students should be able to:

 Prepare calibration curve using excel sheet
 Determine protein concentration using spectrophotometer

Laboratory Session 5-6 Title: Biochemical separation and analysis I

At the end of this lecture, students should be able to:

 Isolate protein present in milk sample and calculate the percentage of protein
 Determine the isoelectric point of casein

Laboratory Session 7-8 Title: Biochemical separation and analysis II

At the end of this lecture, students should be able to:

 Prepare reagents required for the isolation of glycogen
 Isolate glycogen from liver sample
 Determine the percentage of glycogen isolated

Laboratory Session 9-10 Title: Kinetic analysis of enzymes

At the end of this lecture, students should be able to:

 Measure enzyme’s activity
 Determine kinetic parameters Vmax and Km

V. Course General Schedule

A. Lectures
Week # Lecture # Session Titles
1 Introduction to Biological Molecules

1 2 Water & Buffers I

(28 Aug. – 1 Sep.) Water & Buffers II
3
Lab 1: Buffers, PH and molar calculation
2 4 Amino Acids and Polypeptides I

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5 Amino Acids and Polypeptides II

(4 Sep. – 8 Sep.) Protein Primary, Secondary and Tertiary Structures I
6
Lab 1: Buffers, PH and molar calculation
7 Protein Primary, Secondary and Tertiary Structures II

3 8 Protein Primary, Secondary and Tertiary Structures III

(11 Sep. – 15 Sep.) Working With Proteins I
9
Lab 2/Lab 2: Protein assay and calibration curve
10 Working With Proteins II
4 11 Protein Function I: Hemoglobin I
(18 Sep. – 22 Sep.)
Protein Function II: Hemoglobin II
12
National Holiday (21-22 Sep.)
13 Protein Function II: Actin & myosin
5 14 Biosignaling I
(25 Sep. – 29 Sep.)
Biosignaling II
15
Lab 3: Biochemical separation and analysis I
16 Biosignaling III

6 17 Vitamins & Coenzymes

(2 Oct. – 6 Oct.) Bioenergetics I: Thermodynamics
18
Lab 3: Biochemical separation and analysis I
19 Bioenergetics II: High Energy Molecules
20 Enzymes: Structure and Function
7
(9 Oct. – 13 Oct.) Enzymes: Catalysis
21
Lab 4: Biochemical separation and analysis II
MIDTERM EXAM Sunday, 9 October 2022)
22 Enzymes: Kinetics and Inhibition

8 23 Enzymes: Regulation I
(16 Oct. – 20 Oct.) Enzymes: Regulation II
24
Long Weekend 1 ( 16-17 Oct.)
25 Carbohydrates Structure and Functions I
9 26 Carbohydrates Structure and Functions II
(23 Oct. – 27 Oct.)
Lipid Structure and Function I
27
Lab 4: Biochemical separation and analysis II
28 Lipid Structure and Function II
10 29 Nucleic Acids Structure and Function I
(30 Oct. – 3 Nov.)
Nucleic Acids Structure and Function II
30
Lab 5/Lab 5: Kinetic analysis of enzymes
11 REVISION
(6 Nov. – 10 Nov.) Long Weekend 2 ( 10 Nov.)
12
(13 Nov. – 17 Nov.) FINAL EXAM ( Monday 14 November 2022)

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B. Laboratory

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Week Laboratory Activity Title

1-2 Buffers, PH and molar calculation

3-4 Protein assay and calibration curve

5-6 Biochemical separation and analysis I

7-8 Biochemical separation and analysis II

9-10 Kinetic analysis of enzymes

Course Assessment
In order to pass the Course, a student must obtain a minimum final course grade of D. This grade is a
composite of the following Course Assessment requirements

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 Attendance requirement
 Continuous assessment
 End-of-Course assessment

1. Attendance Requirements

Students are required to attend no less than 75% of all educational activities during the Course. This
includes lectures, practical sessions, and case discussion sessions. Students’ attendance will be recorded
during all sessions. Failure to meet this requirement without a valid excuse will result in exclusion from
the final examination.

2. Continuous Assessment (45% )

One written examination will be conducted on week 7 of the course and the content will be related to
lectures. The exam will consist of 40 MCQs and will be given for one hour and a half.

 Midterm Examination will cover lectures from lecture 1 to lecture 16.

3. End-of-course Examination (55%)

The end of course examination consists of two parts: Final Lab and Final Written Examinations. The
content of the final written examination will be related to lectures of the whole course as the following
distribution (25% of the questions on the topics of the first examination and 75 % on the topics of the final
lectures). This assessment will consist of 80 MCQs and will have three-hour duration according to the
table below.

4. Calculation of the Final Grade

The final grade is a composition of the grades obtained for the specified course
requirements, calculated according to the weight. The following table presents an overview
of the course requirements and their weight in the final grade.

Instruments
Course Weight in Final
# of
Requirements Type Duration Course Grade
Questions
Continuous Midterm Exam 40 1.5 hr 30%
Assessment
Lab Report - - 15%

Final Lab Examination 20 1 hr 15%

Final Exam
Final Written Examination 60 2 hr 40%
Total 100%

5. Grading Criteria

The following grading code will be used (in compliance with the system established by King Saud bin
Abdulaziz University for Health Sciences).

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English Grade Code Score Range Equivalent

A+ 95 – 100% Excellent plus
A 90 – 94% Excellent
B+ 85 – 89% Very good plus
B 80 – 84% Very good
C+ 75 – 79% Good plus
C 70 – 74% Good
D+ 65 – 69% High Pass
D 60 – 64% Pass
F < 60% Fail

6. Course Evaluation

 Student Course Evaluation Survey

 Course Meetings Throughout the Semester
 Course Report
 Psychometric Analysis of Exam Results

POLICY FOR MAKE UP EXAMS

(RESCHEDULED EXAM FOR A MISSED EXAM)
POLICIES:

1. MIDTERM EXAM
A. If a student misses a Midterm Exam with a valid and approved excuse/leave:
 He/she will NOT sit for a Make-Up Midterm Exam.

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 The original weight assigned to this missed Midterm Exam will be added to the weight of
the Final Exam of the same course (e.g. If a student misses a midterm worth 20% of the
course, this 20% will be added to the weight of the Final Exam). This re-weighing of the
Final Exam will be permitted ONLY 1(One) Midterm per course.
B. If a student misses a Midterm Exam WITHOUT a valid and approved excuse/sick leave, he/she will
be given a grade of 0 (zero) for the said exam.

2. FINAL LAB/FINAL ORAL EXAM/ IN-CLASS WRITING FINAL

A. If a student misses one of the above exams with a valid and approved excuse/sick leave:
 He/she is eligible to sit for a Make-Up Exam during the Final Exam period.
 The date of this Final Make-Up Exam will be set by the Department.
B. If a student misses any of the above Exams WITHOUT a valid and approved excuse. Sick leave,
he/she will be given a grade of 0 (zero) for this exam.

3. FINAL WRITTEN EXAM

A. If a student misses a Final Written Exam with a valid and approved excuse/ sick leave:
 He/she is eligible to sit for a Make-Up Exam on the Re-Sit Exam date.
 He/ she will not be eligible for an additional Re-Sit Exam if he fails the course.
B. If a student misses a Final Written WITHOUT a valid and approved excuse/sick leave, he/she
will be given a grade of 0 (zero) for the said exam.

NOTE: all excuse /sick leave must be submitted to the Student Affairs Department within five (5)
working days of the original scheduled exam. Late submission will note be
accepted

Academic Integrity Committee

Plagiarism Policy

I. Statement of Philosophy
A. King Saud bin AbdulAziz University for Health Sciences strives to create an environment in
which academic and scholarly integrity is maintained at the highest standards. As such, students are
expected to adhere to these standards and avoid any misconduct that may be in violation of them.
This means that students should be honest with regard to their coursework and avoid plagiarism,
cheating and other forms of academic dishonesty. Academic dishonesty in any form is considered a
serious offense from professional, ethical and religious perspectives.

II. Definition of Plagiarism

A. Plagiarism involves the unauthorized use of someone else's work or ideas and representation of

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them as one's own original work. Work or ideas may be found in any number of sources (e.g.
written text, visual text, spoken text, multimedia products, etc). Any time a student uses another
person's words or ideas without giving them appropriate credit, it is considered plagiarism.
B. The following are considered specific acts of plagiarism (Rockler-Gladen, 2006):
1. Putting one's name on someone else's paper. Examples of this include college essay plagiarism
websites and using term papers from a friend.
2. Putting one's name on someone else's phrases. It isn't necessary to steal a complete paper to be
considered plagiarism. Using just a few sentences or paragraphs from a book or website is
plagiarism if the original author is not credited for the work.
3. Putting one's name on something that is paraphrased. A paraphrase is a rewording of a phrase,
sentence, or paragraph that essentially means the same as the original. Paraphrases of someone
else's work need to be cited just as a direct quote would. Although the words are changed, it is still
someone else's idea and they should be given due recognition. Failure to do this is considered
plagiarism.
4. "Recycling" old material. Slightly modifying the contents of one assignment to meet the
requirements of another assignment is considered to be plagiarism.
5. Failure to put a quote in quotations marks, or providing incorrect information about where a
source came from. Although these may seem to be simple errors they are still counted as
plagiarism.
6. Translating material on a translation website (e.g. Google) and then not providing a reference
for the translation. This is considered to be plagiarism since the work of translating was not the
student's own. A reference for the site from which the translation was obtained should be provided.

III. Consequences of Plagiarism

A. First Offense (Applicable to all Semesters):

1. The student will be given a verbal warning from the course instructor, as well as a brief reminder of
the definition, seriousness, and consequences of plagiarism. The student will be required to repeat
the assignment. A report will be made to the Academic Integrity Committee. The offense will not
be documented in the student's record.

B. Second Offense (Applicable to Semester Two and above):

1. The student’s work will automatically be assigned a score of ‘0’ on the assignment, and he/she will
be referred to the Chairperson of the respective department for further reprimand. A report will be
made to the Academic Integrity Committee and the offense will be documented in the student's
record.

C. Third Offense or Higher (Applicable to Semester Two and above):

1. If the student commits a third offense (or higher), either in the same course or in a subsequent
course, he/she will automatically be assigned a score of ‘0’ on the assignment. The student will be
given a written warning and referred to the Associate Dean (for males) or Assistant Dean (for
females) of the University Pre-Professional Program for further reprimand. A report will be made to

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the Academic Integrity committee and the offense will be documented in the student's record.

IV. Plagiarism Appeals Committee

A. Upon the second (or more) plagiarism offense, the student will have recourse to convene a
committee to appeal the assigned grade of ‘0’ for the work if he/she feels he/she has not plagiarized.
This request must be made in writing and submitted to the Chairperson of the Academic Integrity
Committee within one week of the incident.
B. The committee will be comprised of the Chairperson of the Academic Integrity Committee and three
other instructors. Two of the committee members will be selected from the Academic Integrity
Committee and one from outside of the committee. At least one of the instructors on the Appeals
Committee should be a writing instructor. None of the instructors should be teaching the student at
the time of the offense. In the event that the Chairperson is the instructor of the student, another
committee member will be assigned to chair the committee. 
C. The purpose of this committee will be to make an objective decision as to whether or not the student
has actually produced plagiarized work and to apply the consequences if appropriate. Information
regarding the plagiarism, the plagiarism policy, and the appeals committee will be provided to
students during the orientation process.

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