NAME OF THE COURSE
Code
Course teacher
Medical Chemistry and Biochemistry
MFE201
Year of study
Assist.prof. Vedrana Čikeš
Čulić, PhD
Credits (ECTS)
2nd
17
Assoc.prof. Anita Markotić,
L
S
P
T
PhD; full prof. Irena Drmić
Hofman, PhD; Nikolina
Režić Mužinić, prof. biol.
Type of instruction
Associate teachers
chem.; Angela Mastelić,
(number of hours)
66
60
64
190
mag.ing.mol.biotech.;
Sandra Dujić-Bilušić,
mag.for.chem.mol.biol.
Mandatory
Percentage of
0%
Status of the course
application of e-learning
COURSE DESCRIPTION
Course enrolment
Passed exams from the first year of the Program.
requirements and
entry competences
required for the
course
1. Describe and explain the basic chemical bonds between the compounds and
analyze and calculate the basic physicochemical principles that apply to gases and
solutions
2. Describe and explain the structure and reactions of the most important
biochemical compounds, including small, large and supramolecular structures that
Learning outcomes are found in the cell
expected at the
3. Define and explain the principles of biochemical and energetic changes as well
level of the course
as regulation mechanisms of metabolism of carbohydrates, lipids, proteins,
(4 to 10 learning
informational macromolecules and signaling molecules
outcomes)
4. Integrate the metabolic changes at the cell, tissue, and whole organism level
5. Develop practical skills for working in the laboratory (the basics of safe practice in
the lab, the calculation of basic laboratory parameters and monitoring and
interpretation of results of laboratory measurements
6. Critically judge the meaning of biochemistry in modern medical science
Total number of hours :
LECTURES (L)
SEMINARS (S)
PRACTICALS (P)
TOTAL
Course content
broken down in
detail by weekly
class schedule
(syllabus)
66
60
64
190
In parentheses is the number of hours referred to each topic.
I. MEDICAL CHEMISTRY (MC)
1. GENERAL CHEMISTRY (C1)
Lectures (L)
L1 (2) Introduction into chemical basis of life. Atoms and elements.
L2 (2) Chemical bonds.
L3 (1) Free particles: the nature of gases.
L4 (2) Water and aqueosus solutions. Colligative properties of solutions.
L5 (2) Acids and bases. Buffer solutions.
L6 (2) Colloidal-dispersed systems.
L7 (2) Energy in transition: thermochemistry.
L8 (1) Reactions at equilibrium.
L9 (1) The rate of chemical change.
L10 (1) The natural direction of change: the second law.
L11 (1) Chemical energy and electrical energy: electrochemistry.
Seminar practicals (SP) and practicals (P)
SP1+P1 (1+3) Basic stoichiometry. Preparation of solutions.
SP2+ P2 (1+3) Optical methods in medical chemistry.
SP3+ P3 (1+3) Gas laws. Ions in solution. Osmotic pressure.
SP4+ P4 (1+3) Volumetry: neutralization methods.
SP5+ P5 (1+3) Volumetry: oxidation and reduction method.
SP6+ P6 (1+3) Acids and alkalis, pH and buffers.
SP7+ P7 (1+3) Energetics and kinetics of chemical reaction.
2. ORGANIC CHEMISTRY (C2)
Lectures (L)
L12 (2) Introduction to organic chemistry. Saturated and unsaturated hydrocarbons;
physical and chemical properties. Isomers.
L13 (2) Halogenalkanes; nucleophilic substitution, elimination. Optical isomerism;
relative and absolute configuration.
L14 (1) Alcohols. Ethers. Aldehydes. Ketones.
L15 (2) Carboxylic acids and their derivates.
L16 (2) Cyclic and aromatic hydrocarbons. Sulfuric and heterocyclic compounds.
L17 (1) Amino acids. Carbohydrates.
Seminars organic chemistry (SO)
SO1 (3) Resonant structures. Isomers. Alkanes, alkenes, alkynes. Alkaloids,
phenols, esters, aldehydes. Ketones
SO2 (3) Amines. Sulfur heterocyclic compounds. Amino Acids. Carbohydrates.
Carboxyl compounds
Seminar practicals (SP) and practicals (P)
SP8+ P8 (1+3) Qualitative analysis of some organic compounds
SP9+P9 (1+3) Potentiometric titration of amino acids
II. MEDICAL BIOCHEMISTRY (MB)
Lectures (L) and seminars biochemistry (SB)
BIOCHEMISTRY (B1)
1. STRUCTURE AND FUNCTION OF PROTEINS AND ENZYMES
L18 (2) Amino acids and peptides. Proteins: determination of primary structure.
L19 (2) Proteins: higher orders of structure. Proteins: myoglobin and hemoglobin;
collagen. SB19 (1) Sickle cell anemia. Scurvy.
L20 (2) Enzymes: mechanism of action, kinetics, regulation of activities. SB20 (2)
Izoenzymes. Enzymes in medicine.
2. BIOENERGETICS AND METABOLISM OF CARBOHYDRATES AND LIPIDS
L21 (2) Bioenergetics: the role of ATP. Biologic oxidation. The respiratory chain and
oxidative phosphorylation. SB21 (2) Regulation of respiratory chain.
L22 (1) The citric acid cycle: the catabolism of acetyl-CoA. SB22 (1) Pyruvate
dehydrogenase deficiency.
L23 (1) Glycolysis and the oxidation of pyruvate. SB23 (1) Glycolysis regulation.
L24 (1) Metabolism of glycogen. SB24 (1) Regulation of glycogenesis and
glycogenolysis.
L25 (1) Gluconeogenesis. SB25 (1) Control of blood glucose.
L26 (1) The pentose phosphate pathway. SB26 (1) Other pathways of hexose
metabolism.
L27 (2) Oxidation of fatty acids: ketogenesis. SB27 (1) Metabolic ketoacidosis.
L28 (1) Biosynthesis of fatty acids and eicosanoids. SB28 (1) Lipid transport and
storage.
L29 (1) Cholesterol synthesis, transport and excretion. SB29 (1)
Hypercholesterolemia and synthesis of bile salts and vitamin D.
BIOCHEMISTRY (B2)
3. METABOLISM OF PROTEINS AND AMINO ACIDS
L30 (1) Biosynthesis of the nutritionally nonessential amino acids.
L31 (2) Catabolism of proteins and of amino acid nitrogen. Catabolism of the carbon
skeletons of amino acids. SB31 (1) Regulation of amino acid and protein
catabolism.
L32 (2) Conversion of amino acids to specialized products. Porphyrins and bile
pigments. SB32 (1) Porphyrine metabolism disorders.
4. STRUCTURE, FUNCTION AND REPLICATION OF INFORMATIONAL
MACROMOLECULES
L33 (2) Nucleotides. Metabolism of purine and pyrimidine nucleotides. SB33 (1)
Regulation of purine and pyrimidine metabolism.
L34 (1) DNA organization, replication and repair. SB34 (2) DNA mutations and
chemotherapy.
L35 (1) RNA synthesis, processing and modification. Protein synthesis and the
genetic code. SB35 (1) Protein synthesis regulation and inhibition.
L36 (1) Regulation of gene expression. SB36 (1) Gene expression regulation.
L37 (2) Molecular genetics, recombinant DNA and genomic technology.
5. BIOCHEMISTRY OF EXTRACELLULAR AND INTRACELLULAR
COMMUNICATION
L38 (2) Membranes: structure, assembly and function. SB38 (1) Protein
conformational changes in membrane.
L39 (2) The diversity of the endocrine system. SB39 (1) Hormone synthesis
disorders.
L40 (2) Hormone action and signal transduction. SB40 (1) Signal transduction
disorders.
6. SPECIAL TOPICS
L41 (2) Nutrition, digestion and absorption.
SB41 (1) Micronutrients: vitamins and minerals.
L42 (2) Integration of metabolism. SB42 (1) Integration of tissue metabolism.
Special topics. Additional seminars
SB43 (2) Biochemistry of extracellular matrix. Plasma proteins and
immunoglobulins.
SB44 (2) Hemostasis and thrombosis.
SB45 (2) Metabolisam of xenobiotics.
Seminar practicals (SP) and practicals (P)
SP10+ P10 (1+3)
SP11+ P11(1+2)
SP12+ P12(1+2)
SP13+ P13(1+3)
Serum proteins electrophoresis
Urease: determination of inhibitor
Alkaline phosphatase: effect of pH on enzyme activity
Alkaline phosphatase: determination of Km and Vmax in the
SP14+ P14(1+2)
SP15+ P15(1+3)
SV16+ P16(1+2)
SP17+ P17(1+2)
SP18+ P18(1+2)
SP19+ P19(1+3)
SP20+ P20(1+2)
SP21+ P21(1+3)
SP22+ P22(1+2)
SP23+ P23(1+2)
P24 (4)
Format of
instruction
Student
responsibilities
Screening student
work (name the
proportion of ECTS
credits for each
activity so that the
total number of
ECTS credits is
equal to the ECTS
value of the course)
presence of inhibitors
Amylase: determination in saliva sample
Determination of HbA1c by ion-exchange chromatography
Lipids: separation of skin lipids by thin-layer chromatography
Determination of lipoproteins
Determination of conjugated and total bilirubin in serum
Determination of creatinine and the pathological compounds in
urine
Determination of iron and iron binding capacity in serum
Immmunochemical analysis. ELISA.
Determination of vitamin C
Hemostasis- clotting time and bleeding time tests
Comprehensive final exam (laboratory practicals)
☒ lectures
☒ seminars and workshops
☒ exercises
☐ on line in entirety
☐ partial e-learning
☐ field work
☐ independent assignments
☐ multimedia
☒ laboratory
☐ work with mentor
☒ consultations
In accordance to Rules of studying and Deontological code for USSM students.
Class
attendance
Experimental
work
2
Essay
Research
Practical training 2
Report
(Other)
Seminar
essay
(Other)
Tests
6
Oral exam
(Other)
Written exam
7
Project
(Other)
Grading is based on an absolute scale, with a (minimum) course total of 90
points. Scores in four partial written exams (C1, C2, B1, B2) and a comprehensive
final exam (practicals) are the principal means of accumulating points.
Students who attended lectures and practicals could write partial written exams,
while final exam from practicals is prerequisite for attending B2.
Points can be earned in outside of class activities as well at instructor discretion.
Instructor has the right to deduct points for missed exams, late work, disruptive
classroom behaviour, or lack of effort or participation. Grades are assigned
according to percentage of possible points earned.
Grading and
evaluating student Grading procedures
work in class and at Total accumulated points will be comprised of the following:
the final exam
pass
Physical chemistry (C1)
40
23
Organic chemistry (C2)
15
9
Biochemistry 1 (B1)
50
28
Biochemistry 2 (B2)
40
24
Final exam-practicals
15
9
160
93
Total number of points possible
Final grade in this course will be determined by calculation of mean grade of
the following:
1) C1+C2+ final exam-practicals (max 70 points)
2) B1+B2 (max 90 points)
Point interval of grade 1)
41-48 sufficient (2)
49-56 good (3)
57-63 very good (4)
64-70 excellent (5)
Point interval of grade 2)
52-61 sufficient (2)
62-71 good (3)
72-81 very good (4)
82-90 excellent (5)
Title
Required literature
(available in the
library and via other
media)
1. Murray RK, Bender DA, Boatham KM, Rodwell
VW, Weil PA: Harpers’ Illustrated Biochemistry, 29th
edition. McGraw Hill, 2012.
1. Atkins PW, de Paula J. Physical Chemistry, 10th edition. Macmillian
Education, Oxford, 2014.
2. McMurry JE. Fundamentals of Organic Chemistry, 7th edition. Cornell
University, 2011.
3. Lieberman M, Marks AD. Mark's Basic Medical Biochemistry-a Clinical
Approach, 4th edition. Lippincott Williams & Wilkins, 2013.
Optional literature
(at the time of
submission of study
programme
proposal)
Quality assurance
methods that
ensure the
acquisition of exit
competences
Other (as the
proposer wishes to
add)
Number of
Availability via
copies in
other media
the library
2




Teaching quality analysis by students and teachers
Exam passing rate analysis
Committee for control of teaching reports
External evaluation