Download Biochemistry

THE SYLLABUS OF BIOCHEMISTRY AND
MOLECULAR BIOLOGY
Applicable Students: Six-year system oversea students in the department of
clinical medicine.
Class Hours:
It takes 138 hours to study this course. The study of theory needs 90 hours, the
study of experimental skill needs 48 hours.
Course Introduction:
Biochemistry and Molecular Biology is a required course for basic Medicine.
It can be defined as the science to clarify the phenomenon and the nature of life and
to explain the biochemistry problems about normal human and disease processes at
the molecular level. Biochemistry and medicine are closely linked. Biochemistry is
the basic disciplines which progressed rapidly in the life sciences. Its theory and
technology has penetrated into various fields of other basic medicine and clinical
medicine, and promote many interdisciplinary emerging, such as molecular genetics,
molecular immunology, molecular microbiology, molecular pathology, and
molecular pharmacology. Biochemistry and molecular biology plays a role in
promoting the development of medicine and has become the common language of
the life sciences and frontier disciplines.
Biochemistry and Molecular Biology is to study the structure and function of
biological macromolecules, metabolism and its regulation, genetic information
transfer and its regulation, as well as their role in life activities. With the
development of the medicine, lots of wonders are being created, and explosive
information is being provided at an unprecedented speed. Biochemistry is a window
opening to the world of life science. Thus, the knowledge of biochemistry which
involves the study of chemical molecules and reactions in living organisms, and the
elucidations of the nature of live phenomenon on the molecular level, is essential to
medical students, as well as to the students of other related disciplines.
The Basic Objectives
It will request students to grasp the basic knowledge of Biochemistry and
Molecular Biology, learn to analyze the changes in metabolism and explore the
pathogenesis of the disease at molecular level and use biochemical theory and
technology to solve problems in various disciplines. Simultaneously, through a
variety of teaching and learning activities as much as possible enable students to
familiar with the basic experimental techniques in the field of biochemistry, to
understand the biochemical disciplines important new development, and to train
students’ independent analysis and problem-solving skills. Which would lay a solid
foundation for learning subsequent clinical specialties?
Teaching Hours Distribution
Content
Teaching
hours
Structure and Function of Protein
6
Amino Acids
2
Chapter 2
Peptides
2
Chapter 3
Proteins
2
Nucleotides and Vitamins
1
Nucleotides
1
Enzymes
8
Chapter 8
General Properties of Enzymes
2
Chapter 9
Mechanism of Action of Enzymes and Coenzymes
2
Chapter 10
Kinetics of Enzymatic Reaction
2
Chapter 11
Regulation of Enzyme Activity
2
Part 4
Biological Oxidation
7
Chapter 12
Biological Oxidation
2
Chapter 13
The Respiratory Chain and Oxidative Phosphorylation
2
Chapter 14
Tricarboxylic Acid Cycle
3
Metabolism of Carbohydrates
8
Part 1
Chapter 1
Part 2
Chapter 6
Part 3
Part 5
Chapter 15
Overview of Carbohydrates Metabolism
1
Chapter 16
Glycolysis and Oxidation of Pyruvate
2
Chapter 17
The Pentose Phosphate Pathway
1
Chapter 18
Metabolism of Glycogen
1
Chapter 19
Gluconeogenesis
2
Chapter 20
Control of Blood Glucose
1
Metabolism of Lipid
8
Chapter 22
Overview of Lipids Metabolism
2
Chapter 23
Anabolism of Triacylglycerol
1
Chapter 24
Catabolism of Triacylglycerol
1
Chapter 25
Mebabolism of Phospholips and Sphingolipids
1
Chapter 26
Metabolism of Cholesterol
1
Chapter 27
Transportation and Storage of Lipids
2
Catabolism of Protein
10
Chapter 28
Overview of Catabolism of Protein
2
Chapter 29
Metabolism of Amino Acid Nitrogen
3
Chapter 30
Catabolism of the Carbon Skeletons of Amino Acids
3
Chapter 31
Conversion of Amino Acids to Specialized Products
2
Metabolism of Nucleotides
4
Chapter 32
Metabolism of Purine Nuleotides
2
Chapter 33
Metabolism of Pyrimidine Nucleotides
2
Part 9
Metabolism of Nonnutritive Substances
3
Chapter 34
Biotransformation of Nonnutritive Substances
1
Chapter 35
Metabolism of Porphyrims and Bile Pigments
1
Chapter 36
Bile and Metabolism of Bile Acids
1
Part 10
Regulation
of
Metabolism
Interrelationships of Substance
Part 6
Part 7
Part 8
and
Metabolic
4
Chapter 37
Overview of Metabolism
1
Chapter 38
Regulation of Substances Metabolism
1
Chapter 39
Metaboic Interrelationships of Nutritive Substance
1
Chapter 40
Substances Metabolism in Different Tissues and Organs
1
Gene and Genome
2
Chapter 41
Structure and function of DNA
1
Chapter 42
Structure and function of RNA
Chapter 43
Structure and function of gene
Chapter 44
Structure and function of genome
Part 11
1
Flow of Genetic Information
20
Chapter 45
DNA Synthesis-Replication of Genomic DNA
3
Chapter 46
DNA Damage and Repairing
1
Chapter 47
RNA Synthesis-Transcription
4
Chapter 48
Protein Synthesis-Translation
4
Chapter 49
Basic Concepts and Principles of Regulation and Control
of Gene
2
Chapter 50
Regulation of Gene Expression in Prokaryotes
4
Chapter 51
Regulation of Gene Expression in Eukaryotes
2
Part 13
Cell Communication and Signal Transduction
4
Chapter 52
Molecular Basis of Cell Communication and Signal
Transduction
2
Chapter 53
Signal Transduction Pathway
2
Basic Technology in Molecular Biology
3
Genetic Recombination and Genetic Engineering
3
Gene and Disease
2
Chapter 58
Oncogenes and Antioncogenes
1
Chapter 59
Gene Diagnosis
1
Chapter 60
Gene Therapy
Part 12
Part 14
Chapter 57
Part 15
Total
THEORETICAL PART (90 Hours)
90
PART 1
STRUCTURES AND FUNCTIONS OF
PROTEINS
[Objectives]
1. Master the nitrogen content of amino acids, peptide bond,motif, chaperone,
peptide unit, the classification of amino acids, isoelectric point, the primary，
secondary，tertiary and quaternary structure of protein ,denaturation of protein,
physicochemical properties of protein
2. Understand structure-function relationships of protein, various forces stabilize
protein structure, the role of chaperones in protein folding, the role of
chaperones in protein folding
[Contents]
1. Amino acids
(1) The structure features of amino acids
(2) Amino acids are classified according to the characters of their R groups
(3) The elements of amino acids, the content of nitrogen is relative constant
(16%)
(4) Physicochemical properties of amino acids: isoelectric point, amino acid
may have different charge, ultraviolet absorption, reaction with ninhydrin
(5) The α-group determin the properties of individual amino acids
2. Peptides
(1) L-amino acids linked by peptide bonds form peptides : peptide,
oligopeptide, polypeptide and polypeptide chain, peptide bond
(2) Properties of peptides: glutathione, peptides are polyelectrolytes, pH and
pK determine net charge on peptides
3. Proteins
(1) The classification of proteins: simple proteins and conjugated proteins,
globular proteins and fibrous proteins
(2) Primary structure of protein
(3) Secondary structure of proteins: alpha-helix, the beta sheet, loops and
bends,random coil
(4) Tertiary structure of proteins :super-secondary structure, motif, domain
(5) Various forces stabilize protein structure: salt bridges, hydrophobic
interaction link, hydrogen bond, van der waals force, disulfied bonds
(6) The role of chaperones in protein folding
(7) Quaternary structure of protein
(8) Denaturation of proteins: denaturation, renaturation
(9) Physicochemical properties of protein: proteins have different charge,
proteins are colloid molecules, ultraviolet absorption, color reaction
PART 2
NUCLEOTIDES AND VITAMINS
[Objectives]
1. Master the elemental and molecular components of nucleic acid, the function of
nucleic acids; nucleic acids contain five major heterocyclic bases and rare
bases.
2. Understand the numbering systems, purines and pyrimidines are planar
molecules,
[Contents]
Nucleotides:
(1) General introduction of nucleic acids and nucleotides: there are two nucleic
acids:DNA and RNA, the elemental and molecular components of nucleic
acid, the function of nucleic acids.
(2) Chemistry of purines and pyrimidines : they are heterocyclic compounds,
the numbering systems, purines and pyrimidines are planar molecules,
nucleic acids contain five major heterocyclic bases and rare bases.
(3) Nucleosides and nucleotides: nucleosides contain monosaccharides,
nucleotides are phosphorylated nucleosides, some important nucleotides
PART 3
ENZYMES
[Objectives]
1. Master characteristics of enzymatic reactions, moleculare constituents of
enzyme , isoenzyme, influences of substrate concentration, enzyme
concentration, temperature, pH, inhibitors, activators on the activity of enzymes,
regulation of the activity of enzymes
2. Understand nomenclature of enzyme、
classification of the enzyme,mechanism of
action of enzymes.
[Contents]
1. General properties of Enzymes:
(1) Enzyme are efficient biocatalysts : the conception of enzyme, ribozyme
(2) Enzyme are of important biological significances
(3) Characteristics of enzymatic reactions: highly efficient, high specificity, the
regulation of the enzyme
(4) Moleculare constituents of enzyme : simple enzyme and conjugated
enzyme, the conception of holoenzyme、apoenzyme 、prosthetic groups
(5) Nomenclature of enzyme : customary and systematic nomenclature of
enzyme
(6) Enzymes are classified by the reactions they catalyze
(7) Isoenzyme are distinct forms of enzyme with the same catalytic activity :
the conception of the isoenzyme
2. Mechanism of action of enzymes and coenzymes
(1) Why a chemical reaction can take place
(2) Enzymes speed up the rates by lowering the activation energy without
influencing the equilibrium of a reaction
(3) Enzyme binds substrate and catalyzes the conversion of substrate to
product
(4) Enzymes catalyze the reactions through different mechanisms : chemical
catalysis, general acid-base catalysis, covalent catalysis, metal ion catalysis,
catalysis by strain
(5) The function of coenzymes, prosthetic group and cofactors : cofactor
contain : B vitamins , TPP, FMN, FAD ,NAD+, NADP+, CoA, THF, acyle
group.
3. Kinetics of enzymatic reactions
(1) How to measure the activity of enzymes
(2) What is the kinetics of enzymatic reaction
(3) Substrate concentration influences the rate of enzymatic reactions:
michaelis equation, Km and Vmax.
(4) Enzyme concentration influences the rate of enzymatic reactions
(5) Temperature influences the rate of enzymatic reactions : optimum
temperature
(6) pH value influences the rate of enzymatic reactions: pH optimum
(7) Influences of inhibitors on the activity of enzymes: irreversible inhibition
of
enzyme
activity,
reversible
inhibition,
competitive
inhibiton,
non-competitive inhibition, uncompetitive inhibition.
(8) Influences of activators on the activity of enzymes
4. Regulation of enzyme activity
(1) Key enzyme
(2) Regulation of the activity of enzymes
(3) The quantity of enzyme is modulated by regulating the rate of synthesis
and /or degradation
PART 4
BIOLOGICAL OXIDATION
[Objectives]
1. Master the components of the respiratory chain : complex Ⅰ、Ⅱ、Ⅲ、Ⅳ, two
respiratory chains: NADH respiratory chain and FADH2 respiratory chain, the
inhibition
of
the
respiratory
malate-aspartate shuttle,
chain,
α-glycerophosphate
shuttle
and
TAC consists of eight reactions, the regulation of the
TAC, the key enzymes of the TAC : citrate synthase, isocitrate dehydrogenase
andα-ketoglutarate dehydrogenase, physiological significance of TAC
2. Understand biomedial importance of biological oxidation, oxidases use oxygen
as a hydrogen acceptor, hydroperoxidases use hydrogen peroxide or anorganic
peroxide as substrate, oxigenases catalyze the direct transfer and incorporation
of oxygen into a substrate molecule, superoxide dismutase protects aerobic
organisms against oxygen toxicity
[Contents]
1. Biological oxidation
(1) Biomedial importance of biological oxidation
(2) Oxidases use oxygen as a hydrogen acceptor
(3) Hydroperoxidases use hydrogen peroxide or anorganic peroxide as
substrate
(4) Oxigenases catalyze the direct transfer and incorporation of oxygen into a
substrate molecule
(5) Superoxide dismutase protects aerobic organisms against oxygen toxicity
2. The respiratory chain and oxidative phosphorylation
(1) Storage and utilization of energy in vivo
(2) The respiratory chain collects and oxidizes reducing equivalents: the
components of the respiratory chain ,complex Ⅰ、Ⅱ、Ⅲ、Ⅳ.
(3) There are two respiratory chains: NADH respiratory chain and FADH2
respiratory chain
(4) The respiratory chain provides most of the energy captured in metabolism
(5) The chemiosmotic theory explains
the mechanism
of oxidative
phosphorylation
(6) Many poisons inhibit the respiratory chain: H2S, carbon monoxide,
cyanide,oligomycin
uncouplers
(7) The relative impermeability of the inner mitochondrial membrane
necessitates exchange transporters: α-glycerophosphate shuttle and
malate-aspartate shuttle.
3. Tricarboxylic acid cycle
(1) The tricarboxylic acid cycle is an important stage for cellular respiration
(2) The tricarboxylic acid cycle consists of eight reactions
(3) TAC is regulated by the regulation of the activity of key enzymes:citrate
synthase, isocitrate dehydrogenase andα-ketoglutarate dehydrogenase
(4) Physiological significance of TAC
PART 5
METABOLISM OF CARBOHYDRATES
[Objectives]
1. Master the reactions and enzymes in clycolysis, regulation of glycolysis,
physiologic significance of glycolysis, and production of ATP from catabolism
of glucose, glycogenesis and glycogenolysis pathway, gluconeogenesis
pathway, control of the blood glucose by hormones: insulin and glucagon.
2. Understand oview of carbohydrates metabolism, classification of carbohydrates,
and physiologic significance of carbohydrates, digestion and absorption of
carbohydrates, the pentose phosphate pathway, physiological significance of
stable level of blood glucose, carbohydrate metabolism in mature red blood
cell.
[Contents]
1. Overview of carbohydrates metabolism
(1) Carbohydrates are aldehyde or ketone derivatives of polyhydric alcohols
(2) There are four main classes of carbohydrates: monosaccharides ,
oligosaccharides, polysaccharides, glycoconjugates
(3) Physiologic significance of carbohydrates: major source of energy, provide
materials for synthesis of other substance, serve as the structural
components.
(4) Digestion and absorption of carbohydrates
(5) Main metabolic pathways of carbohydrate metabolism
2. Glycolysis and the oxidation of pyruvate
(1) Glycolysis can function under anaerobic condition
(2) Reactions and enzymes in clycolysis: two stages: the glycolytic pathway
and the reduction of pyruvate .
(3) Regulation of glycolysis : phosphofructokinase-1, hexokinase and pyruvate
kinase are the key enzyme
(4) Physiologic significance of glycolysis
(5) The oxidation of pyruvate to acetyl-CoA is the irreversible rout from
glycolysis toTAC
(6) Production of ATP from catabolism of glucose
3. The pentose phosphate pathway
(1) Characteristics of pentose phosphate pathway
(2) The reaction of the pathway may be divided into two phases
(3) Regulation of pentose phosphate pathway
(4) Physiologic significance of the pathway
4. Metabolism of Glycogen
(1) Glycogen
(2) Glycogenesis occurs mainly in liver and muscle
(3) Glycogenesis pathway: four basic reaction
(4) Glycogenolysis is not the reverse of glycogenesis but is a separete pathway
(5) Regulation of glycogenolysis and glycogenesis
5. Gluconeogenesis
(6) Gluconeogenesis pathway
(1) Glycolysis and gluconeogenesis were regulated reciprocally
(2) Physical significance of gluconeogenesis
6. Control of the blood glucose
(1) The concentration of blood glucose is regulated within narrow limits
(2) Physiological significance of stable level of blood glucose
(3) Blood glucose is derived from the diet, gluconeogenesis , and
glycogenolysis
(4) Control of the blood glucose by hormones: insulin and glucagon
7. Carbohydrate metabolism in mature red blood cell
(1) The red blood cells has a unique and relatively simple metabolism
(2) The glucose transporter in red blood cell membrane
(3) Metabolic pathway of glucose in red blood cells
(4) The function of ATP in red blood cells
(5) The function of 2,3-BPG in red blood cells
(6) The function of NADPH and NADH
(7) Deficiency of G-6-P dehydrogenase may cause hemolytic anemia
PART 6
METABOLISM OF LIPID
[Objectives]
1. Master lipogenesis: de novo synthesis of fatty acids , biosynthesis of
triacylglycerol, essential fatty acids , oxidation of fatty acids, ketogenesis,
synthesis of cholesterol ,conversion of
cholesterol
2. Understand overview of lipid metabolism, eicosanoids are formed from C20
polyunsaturated fatty acids, synthesis of unsaturated fatty acids,
metabolism
of phospholipids an sphingolipids, regulation of cholesterol synthesis ,
transportation and storage of lipids.
[Contents]
1. Overview of Lipid Metabolism
(1) Physiological importance of lipids
(2) Lipids are classified as simple or complex
(3) Fatty acids are aliphatic carboxylic acids
(4) Triacylglycerols are the main storage forms of fatty acids
(5) Phospholipids are the main lipid constituents of membranes
(6) Steroids play many physiological importance roles
(7) Digestion and absorption of lipids
(8) Lipids are metabolized in different ways in vivo
(9) Lipids metabolism in mature red blood cells
2. Anabolism of Triacylglycerol
(1) Lipogenesis : de novo synthesis of fatty acids
(2) Synthesis of unsaturated fatty acids
(3) Regulation of lipogenesis
(4) Biosynthesis of triacylglycerol
(5) Essential fatty acids
(6) Eicosanoids are formed from C20 polyunsaturated fatty acids
3. Catabolism of Triacylglycerol
(1) Catabolism of acylglycerols is not the reversal of biosynthesis of fat
(2) Oxidation of fatty acids occurs in mitochondria
(3) Oxidation of some fatty acids
(4) Ketogenesis
(5) Ketogenesis is regulated at three crucial steps
4. Metabolism of Phospholipids and Sphingolipids
(1) Biosynthesis of phospholipids
(2) Phospholipases allow degradation and remodeling of phosphoglycerides
(3) All sphingolipids are formed from ceramide
5. Metabolism of Cholesterol
(1) Biomedical importance of cholesterol
(2) Cholesterol is derived about equally from the diet and from biosynthesis
(3) Synthesis of cholesterol
(4) Regulation of cholesterol synthesis
(5) Conversion of cholesterol
6. Transportation and Storage of Lipids
(1) Lipids are transported in the plasma as lipoproteins
(2) Free fatty acids are rapidly metabolized
(3) Triacylglycerol is transported in chylomicrons from the intestines
(4) Triacylglycerol is transported in VLDL from the liver
(5) CM and VLDL are rapidly catabolized
(6) LDL is metabolized via the LDL receptor
(7) HDL takes part in metabolism of both triacylglycerol and cholesterol in
lipoproteins
(8) Abnormal metabolism of plasma lipoproteins
PART 7: CATABOLISM OF PROTEINS
[Objectives]
1. Master Transamination, Oxidative deamination of L-glutamate , Combined
deamination, Glutamine synthetase, Biosynthesis of urea, α-keto acids can be
converted into nonessential amino acids and to substrates for carbohydrate and
lipid biosynthesis, Catabolism of sulfur-contanining amino acids、aromatic
amino acids 、branched-chain amino acids
2. Understand overviwe of catabolism of proteins，Conversion of amino acids to
specialized products.
[Contents]
1. Overviwe of Catabolism of Proteins
(1) Importance of protein nutrition
(2) Digestion of proteins from food
(3) Absorption of digested products
(4) Putrefaction of proteins in the large intestine
(5) Protein turnover occurs in all froms of life
(6) Degradation of proteins in vivo
(7) Metabolic pathways of amino acids
2. Metabolism of Amino Acid Nitrogen
(1) Transamination
(2) Oxidative deamination of L-glutamate
(3) Combined deamination
(4) Ammonia intoxication is life-threatening
(5) Glutamine synthetase fixes ammonia as glutamine
(6) Urea is the major end products of nitrogen catabolism in humans
(7) Biosynthesis of urea
(8) Carbamoyl phosphate synthaseⅠ is the pacemaker enzyme of the urea
cycle
(9) Genetic defects in the cycle can be life-threatening
3. Catabolism of the Carbon Skeleton of Amino Acids
(1) α-keto acids can be converted into nonessential amino acids by amination
(2) α-keto acids are catabolized to substrates for carbohydrate and lipid
biosynthesis
(3) Catabolism of sulfur-contanining amino acids
(4) Catabolism of aromatic amino acids
(5) Catabolism of branched-chain amino acids
4. Conversion of Amino Acids to Specialized Products
(1) Many physiological substrances can be produced from amino acids
(2) Metabolism of one-carbon unit
PART 8: CATABOLISM OF NUCLEOTIDES
[Objectives]
1. Master de novo synthesis 、 salvage synthesis pathway of purine and
pyrimidine nucleotides, antimetabolites of purine and pyrimidine nucleotides,
catabolism of purine and pyrimidine nucleotides,
2. Understand Nucleotides are of physiological importance but dietarily
nonessential，interconversion of purine nucleotides , reduction of NDPs forms
dNDPs，The synthesisi of purine and pyrimidine nucleotide are regulated.
[Contents]
1. Metabolism of Purine Nucleotides
(1) Nucleotides are of physiological importance but dietarily nonessential
(2) De novo synthesis of purine nucleotides in vivo
(3) The synthesisi of purine nucleotide is stringently regulated
(4)
“Salvage”
reactions
convert
purines
and
their
nucleosides
to
mononucleotides
(5) Interconversion of purine nucleotides
(6) Reduction of NDPs forms dNDPs
(7) Antimetabolites of purine nucleotides
(8) Catabolism of purine nucleotides
2. Metabolism of Pyrimidine Nucleotides
(1) De novo synthesis of pyrimidine nucleotides
(2) Pyrimidine ribo and deoxyribonucleosides are salvaged
(3) Antimetabolites of pyrimidine nucleotides
(4) Catabolism of pyrimidine nucleotides
PART 9: METABOLISM OF NONNUTRITIVE
SUBSTANCES
[Objectives]
1. Master botransformation of substances by oxidation、reduction 、hydrolysis 、
conjugation reactions, heme is synthesized from succinyl-CoA and glycine, bile
acids are formed from cholesterol, entertohepatic circulation
2. Understand various factors affects the activities of the enzymes metabolizing
xenobiotics , structure of porphyrins , formation、transportation and metabolism
of bilirubin.
[Contents]
1. Biotransformation of Nonnutritive Substance
(1) Biotransformation
(2) Biotransformation of substances by oxidation
(3) Biotransformation of substances by reduction
(4) Biotransformation of substances by hydrolysis
(5) Conjugation reactions prepare the substances for excretion in phase two of
their metabolism
(6) Various factors affects the activities of the enzymes metabolizing
xenobiotics
2. Metabolism of Porphyrins and Bile Pigments
(1) Porphyrins and bile pigments
(2) Structure of porphyrins
(3) Heme is synthesized from succinyl-CoA and glycine
(4) Formation and transportation of bilirubin
(5) Metabolism of bilirubin
(6) Hyperbilirubinemia causes jaundice
3. Bile and Metabolism of Bile Acids
(1) Bile
(2) Bile acids
(3) Bile acids are formed from cholesterol
(4) Most bile acids reture to the liver in the entertohepatic circulation
Part10: REGULATION OF METABOLISM AND
METABOLIC INTERREGULATIONSHIPS OF
SUBSTANCE
[Objectives]
1. Master the general characteristics of metabolism, allosteric regulation and
chemical modification of key enzymes , regulation of the amount of enzyme,
regulation of metabolism by hormones, metabolic conversion of carbohydrates ,
lipids and proteins, function of liver in substances metabolism
2. Understand separate distribution and regulatin of enzymes in cell , integration
regulation of substances metabolism, substance metabolism in different tissues
and organs.
[Contents]
1. Overview of Metabolism
(1) Integration of metabolism
(2) TAC is the common pathway for the catabolism of carbohydrates fat and
proteins
(3) NADPH provides the reducing equivalent needed for anabolism
(4) The purpose of all metabolic pathways of energy metabolism is to maitain
ATP and /or glucose supplies
(5) Metabolism is regulable
(6) Metabolism is different tissues and organs has different characteristics
(7) Each metabolite has a common metabolic pool
2. Regulation of Substance Metabolism
(1) Separate distribution and regulatin of enzymes in cell
(2) Allosteric regulation of key enzymes
(3) Chemical modification of key enzymes
(4) Regulation of the amount of enzyme
(5) Regulation of metabolism by hormones
(6) Integration regulation of substances metabolism
3. Metabolism Interrelationship of Nutritive Substance
(1) Interrelationships of anabolism and catabolism
(2) Interrelationships of nutrient substances in energy metabolism
(3) Metabolic conversion of carbohydrates, lipids and proteins
(4) Not all major substances in metabolism are interconvertible
(5) Some nutritive substances are needed for the metabolic alteration of
nonnutritive substance
4. Substance Metabolism in Different Tissues and Organs
(1) Characteristics of substances metabolism in different tissues and organs
(2) Function of liver in substances metabolism
Part 11: GENE AND GENOME
[Objectives]
1. Master the molecular component of DNA and RNA， the defination of DNA
denaturation, DNA renaturation, hyperchromicity, Tm; structural gene, gene
expression,
operon,
polycistron,
monocistron,
genome.
The
structural
characteristics and functions of mRNA, tRNA, rRNA; the characteristics of
eukaryotic genome.
2. Understand the link bonds between nucleotids; Eukaryotic genes contain many
regulatory elements: promoter, enhancer, silencer and other respons element,
Basic structure characteristics of prokaryotic genes:polycistronic mRNA,
operon.
[Contents]
1. Structure and Funtion of DNA
(1) Structure of DNA: primary structur : sequence of nucleotide, secondary
structure: double helix model
(2) Characteristics of DNA: denaturation and renaturation of DNA
(3) The function of DNA: contains genetic information
(4) Specific nulease digest DNA: endonucleases
2. Structure and Function of RNA
(1) The chemical nature of RNA differs from that of DNA
(2) RNAis organized in several unique structures: mRNA, tRNA, rRNA, small
stable RNA.
(3) The function of RNA
(4) Specific nulease digest RNA: RNase
3. Structure and Function of Gene
(1) Gene is the fundamental genetic unit
(2) Gene contains protein and RNA coding region and regulatory elements
(3) Genetic information is transmitted according to the central dogma
(4) Basic structure characteristics of prokaryotic genes:polycistronic mRNA,
operon
(5) Basic structure characteristics of eukaryotic genes:monocistronic mRNA,
split gene
(6) Eukaryotic
genes
contain
many
regulatory
elements:
promoter,
enhancer,silencer and other respons element
(7) Characteristics of sturcture of virus gene
4. Structure and function of genome
(1) Different organisms have obviusly different genomic features
(2) Basic characteristics of viral genomes
(3) Differnet virus have different nucleic acids as their genome
(4) Introduction of some typical viral genomes
(5) The prokaryotic genomes are relatively complex
(6) Genome of eukaryotes are more complex
(7) Repetitive sequences in human genome
(8) Gene families
(9) The human genome progect
Part 12: FLOW OF GENETIC INFORMATION
[Objectives]
1. Master the definition of Semi-Conservative Replication, Okazaki fragments,
Telomere, Telomerase, Mutation, Reverse transcriptase and the characteristics
of replication, the elements to participate and coordinate in the replication, the
structure and function of Telomere and Telomerase.
2. Understand the the reaction catalyzed by Reverse transcriptase and the
Significance of Reverse transcriptase, the types of Mutation and the DNA
repairing forms.
[Contents]
1. DNA synthesis---- Replication of Genomic DNA
(1) DNA replication is the process in which the whole genomes is synthesized
(2) DNA replication follows a set of fundamental rules: semi-conservative,
bidrectionally, semi-discontinuous, fidelity.
(3) DNA replication reaction is catalyed by DNA polyerase and requires many
other enzyme and protein factors
(4) DNA replication in prokaryotic cells
(5) DNA replication in eukaryotic cells: telomere and telomerase
(6) Reverse transcription
2. DNA Damage and Repairing
(1) DNA damage can result from many factors
(2) DNA damage inclueds different types of alteration of DNA sequences
(3) All celles have mutiple DNA repair systems:photoreactivation repair,
mismatch repair, excision repair, recombination repair, SOS repair.
(4) DNA damage may result in mutations:point mutation,deletion and insertion,
translocation.
CHAPTER 47: RNA SYNTHESIS---TRANSCRIPTION
[Objectives]
1. Master the similarity and differences between replication and transcription, the
composition of RNA-pol of E. Coli, the definition of Asymmetric transcription,
Exon, Intron, Split gene; the Post-Transcriptional Modification of mRNA.
2. Understand the the function of core enzyme and holoenzyme; the definition of
Template strand, Coding strand, and Ribozyme
[Contents]
1. Gene expression
2. RNA is synthesized from a DNA template by an RNA polymerase
3. The initiation of transcription involves the binding of RNA polymerase to
promoter
4. RNA synthesis proceeds in stages:iniation, elongation, termination.
5. RNA synthesis in prokayotic cells
6. RNA synthesis in eukaryotic cells
7. Many RNA molecules are processed before they become funtional
(1) Eukaryotic mRNAis modified at the 5’ and 3’ ends: 5’ cap and 3’ tail
(2) Splicing is needed for the fomation of the mature Mrna
(3) RNA editing
8. The processing of rRNA and tRNA
CHAPTER 48: PROTEIN SYNTHESIS----TRANSLATION
[Objectives]
1. Master the multiple elements to participate and coordinate in the protein
synthesis, the function of mRNA, tRNA, rRNA, the properties of genetic codon;
the definition of Genetic codon, Chaperons; the steps of ribosomal cycle
2. Understand the the function of aminoacyl-tRNA synthetase; the definition of
S-D sequence, Signal peptide, the macromolecules assisting the protein folding.
[Contents]
1. Many substances are involved in the process of translation: ribosome, mRNA,
tRNA, amino acid, special enzymes, ATP, GTP.
2. mRNA molecule contains codons that specify the amino acid sequence of
protein：universal, commaless, wobble, degeneracy
3. The attchment of amino acids to specific tRNAs is catalyzed by
aminoacyle-tRNA synthetases
4. Basic process of protein synthesis in prokaryotes:
(1) Initiation: IF1,IF2, IF3
(2) Enlongation: ribosomal cycle: the entry of aminoacyle-tRNA into the A site,
transpeptidation, translocation; EF-T
(3) Termination: RF
5. Basic process of protein synthesis in eukaryotes
6. Posttranslational process:
(1) primary sturcture processing
(2) higher structures processing: chaperone
(3) amino acid modified
7. Directed transportation of protein
8. Some antibiotics work because they selectively inhibit protein synthesis
CHAPTER 49-50: GENE EXPRESSION REGULATION
[Objectives]
1. Master the definition of Gene expression, Temporal and Spatial specificity of
gene expression, Constitutive expression, Cis-acting elements, trans-acting
factors, Promoter, Operon;, the Structural features of Eukaryotic gene, the
varieties and function of Eukaryotic promoters.
2. Understand the the definition of Gene, Genome, housekeeping genes, Antisense
RNA; the properties of Prokaryotic transcription regulation; the Structural
features of General transcription factors(TF), DNA-binding domain(Zinc finger,
Leucine zipper, Helix-loop-helix)
[Contents]
1. Basic concepts and principles of regulation and control of gene expression
(1) Genes are expressed with temporl speciticity and spatial specificity
(2) The manners of gene expression:constitutive gene expression, induction,
repression
(3) Transcription is the main level for regulation and control of gene
expression: RNA polymerase, cis-actiong elements and trans-actiong
factors
(4) Regulatory proteins have discrete DNA-bingding domains: helix-turn-helix,
zinc finger, helix-loop-helix, leucine zipper
2. Characteristics of regulation of transcription in prokaryotes: lac operon
3. Regulation of gene expression in eukaryotes
(1) regulation and control on transcription in initiation: TF, polⅡ, pomoter
(2) post-transcriptional regulation and control: end modification, alternative
splicing
PART 13: CELL COMMUNICATION AND SIGNAL
TRANSDUCTION
[Objectives]
1. Master the definition of Second messenger, Receptor; the structural properties of
G Protein-Coupled Receptors and Tyrosine protein kinase Receptor, the
definition and structural properties of G protein, the Properties of binding of
receptor and ligand; cAMP dependent-protein kinase A pathway, cGMP
dependent PKG pathway, Ca2+ dependent PK pathway, Tyrosine protein
Kinase pathway and Intracellular receptor pathway.
2. Understand the the definition of Extracellular molecules, most of the Membrane
receptors are Glycoprotein and almost all the Intracellular receptors are DNA
binding protein.
[Contents]
1. Molecular basis of cell communication and signal transduction
(1) Main manners of communication between cells: gap junctions, contact with
molecules on the surface of cell membrane, chemical singals
(2) Types and characteristics of chemical signals
(3) Receptors
1). Four
types
of
receptors:
intracellular
receptors,
membrane
receptors( ion channel receptors, G protein-coupled receptors,
enzyme-linked receptors)
2). Second messengers and signal tranducers in cells: second messengers,
protein kinase, G proteins, adaptor protein
3). Basic manners of signal transduction in cells
2. signal transduction pathways
(1) Signal transduction mediated by intercellular receptors
(2) Signal transduction mediated by Ion-Channel receptors
(3) Signal transduction mediated by G protein-coupled receptors
1). AC-CAMP-PKA pathway
2). GC-CGMP-PKG pathway
3). Ca2+-PKC
pathway
4). Tyrosine protein Kinase pathway
5). JAK-STAT pathway
6). NF-κB pathway
PART 14: TECHNOLOGY IN MOLECULAR BIOLOGY
[Objectives]
1. Master the definition of DNA recombination, Homologous Recombination,
DNA Cloning, Restriction endonuclease, Palindrome; the principle and the
process of DNA cloning
2. Understand the definition of Molecular hybridization, Genetic Engineering,
target gene, Vector, cDNA; the principle of southern blotting, northern blotting,
and western blotting, the principle of DNA sequencing; the types of DNA
recombination in nature.
[Contents]
1. Molecular hybridization of nucleic acids
2. Polymerase chain reactin : denaturation, annealing and extension
3. DNA sequencing
4. Genetic recombination and genetic engineering
(1) Recombination of DNA: homologous recombination, conjugation,
transformation, site-specific rebombination, transposon
(2) Concepts involved in DNA recombination: clone, restriction enzymes,
vectors
(3) Basic principles of DNA recombination
(4) Expression of the cloned gene
PART 15: GENE AND DISEASE
[Objectives]
1. Master the definition of oncogene, anti-oncogene , virus oncogene (v-onc),
cellular- oncogene (c-onc); the Mechanisms of Oncogene Activation, the
Mechanism of action of P53 gene.
2. Understand the definition of and growth factor, gene diagnosis, gene therapy;
the expression products and function of oncogene; main stratrgies of gene
therapy and basic techniques used for gene inactivation/suppression.
[Contents]
1. Oncogene and anti-oncogenes
(1) viral oncogene and cellular oncogene
(2) Function of the products of oncogenes: growth fctors, receptors of growth
factors, G-proteins, protein kinase, DNA binding proteins.
(3) Maligant activation of oncogenes
(4) Anti-oncogene: P53 gene, Rb gene
2. Gene Diagnosis
(1) Basic techniques used for gene diagnosis
(2) Basic methods used for gene diagnosis
(3) Application of gene diagnosis
3. Gene Therapy
(1) Main stratrgies of gene therapy
(2) Basic techniques used for gene inactivation/suppression: siRNA, anti-sense
RNA
Experimental skill
NO.
1
Experimental Skill Name
Protein Salt Precipitation
Hours
4
2
Determination of serum Proteins
4
3
Km Assay of alkaline phosphatase (AKP)
4
4
The measurement of the blood sugar
4
The Function of Lactate Dehydrogenase（LDH）and coenzymeⅠ
4
6
Mensuration of GPT activity in serum
4
7
Polymerase Chain Reaction(PCR) and agarose Gel electrophoresis
8
8
Purification of Urase through the Gel filtration
8
9
Polyacrylamide Gel Disc Electrophoresis（PAGE） of Serum Protein
8
5
Total
48
REFERENCES
1. Harper’s Biochemistry, Ed. R.K. Murray, D.K. Granner, P.A. Mayes and V.W.
Rodwell, Appleton and Lange, Stamford, Connecticut
2. Principles of Biochemistry, Ed. Lehinger, Nelson and Cox. CBS Publishers and
Distributors
3. Biochemistry Ed, Lubert Stryer, W.H. Freeman and Company, New York