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What will be tested in "338 Biochemistry" of Shandong University in 2022?
Shandong University is a key comprehensive university directly under the Ministry of Education with a long history, complete disciplines, strong strength and distinctive features. It has important influence at home and abroad. In 20 17, it successfully entered the ranks of world-class universities (Class A). Shandong University is both a 985 project and a 2 1 1 project. As the top 30 universities in China, Shandong University will take a look in 2022.

● school profile, Shandong University

Founded in 190 1, Shandong University is known as the earliest modern higher education university in China. Its medical discipline originated from 1864, which opened modern higher medical education in China. Since its birth, the school has experienced several historical development periods, such as Shandong University Hall, National Qingdao University, National Shandong University, Shandong University and the new Shandong University formed by the merger of former Shandong University, Shandong Medical University and Shandong Polytechnic University. Since 120, Shandong University has always adhered to the mission of "storing talents for the world and enriching Qiang Bing", deeply practiced the spirit of "endless learning and lofty aspirations", made unremitting efforts, passed down from generation to generation, accumulated and formed the school spirit of "advocating truth, seeking truth from facts and being innovative", trained more than 600,000 talents of all kinds, and made contributions to national and regional economic and social development.

The nature, purpose and content of the "338 Biochemistry" exam.

First, the nature of the examination.

The entrance examination of biochemistry is a level examination for our school to recruit graduate students in life sciences. The examination of this course can truly reflect the candidates' mastery of the basic concepts and theories of biochemistry and their ability and level of comprehensively applying the knowledge they have learned to analyze and solve related problems, which can be used as an important basis for selecting and allocating graduate students in our school.

Second, the examination requirements

The purpose of biochemistry examination is to examine the examinee's mastery of basic knowledge and basic theory of biochemistry. On the basis of examining the examinee's mastery of basic theoretical knowledge, it focuses on the examinee's ability to analyze and solve problems by using basic knowledge of biochemistry.

Third, the examination form and examination paper structure

1. Examination method: closed book and written test.

2. Examination time: 180 minutes.

3. Type of problem

It mainly includes noun explanation, judgment, short answer, calculation and analytical answer.

Fourth, the content of the exam

The examination will cover the following contents of biochemistry: (1) the structure, composition, properties and functions of biomolecules; (2) separation and analysis methods of biomolecules, especially biomacromolecules; (3) the transformation, utilization and regulation of energy in organisms; (4) Decomposition and anabolism of biological macromolecules; (5) Basic theories such as replication, transcription, expression and regulation of bioinformatics molecules. And examine students' comprehensive analysis ability in applying the above knowledge. The basic contents of each part are as follows:

Sugar biochemistry

1. monosaccharide

2. Structure, properties, conformation, configuration and rotation of monosaccharides.

oligose

4. Polysaccharides

(2) Lipid biochemistry

1. triglyceride

2. Structure and properties of triglycerides, saponification value (valence), acid value (valence), iodine value (valence) and acetylation value (valence).

3. Classification, nature and function

4. Binding ester

5. Sterol compounds

(3) protein chemistry

1. Important functions and elements of protein.

2. Important functions of protein;

3. Elemental composition of protein

4. Amino acids

5. Structural characteristics and classification of amino acids;

6. Essential amino acids;

7. Rare amino acids in protein

8. Non-protein amino acids;

9. The nature of amino acids

10.peptide

1 1. peptide bonds and peptide chains;

12. Naming and structure of peptide;

13. Natural bioactive oligopeptide

14. Molecular structure of protein

15. Primary structure of protein;

16. Secondary structure of protein

17. Supersecondary structure and domain

18. The tertiary structure of protein

19. The four-level structure of protein

20. The relationship between protein's structure and function.

2 1. Relationship between primary structure and function of protein

22. The relationship between spatial structure and function of protein.

23. The important nature of protein

24. Gender and isoelectric point in protein;

25. Colloidal properties of protein and protein precipitation.

26. denaturation and renaturation of protein;

27. protein's color reaction

28. Classification of protein

29. Isolation, purification and molecular weight determination of protein.

30. Separation and purification of protein.

3 1. Determination of molecular weight of protein

(4) Nucleic acid chemistry

1. Types and distribution of nucleic acids

2. Chemical composition of nucleic acid

3. deoxyribonucleic acid

Basic composition of 4.4. DNA

The primary structure of 5.5. DNA

The spatial structure of 6.6. DNA

The three-level structure of 7.7. Deoxyribonucleic acid

8. RNA

The structure of 9.9. ribonucleic acid

10. Physical and chemical properties of nucleic acids

1 1. General physical properties;

12. Ultraviolet absorption of nucleic acid;

13. sedimentation characteristics of nucleic acid;

14. Amphoteric dissociation and gel electrophoresis of nucleic acids;

15. denaturation and renaturation of nucleic acids

(5) Enzymology

Introduction to enzymology

2. The concept of enzyme;

3. Catalytic characteristics of the enzyme;

4. Composition of enzyme;

5. Substrate specificity of enzyme

6. Naming and classification of enzymes

7. Factors affecting the speed of enzymatic reaction

8. Determination of enzymatic reaction speed;

9. Effect of substrate concentration on enzymatic reaction speed

10. Effect of enzyme concentration on enzymatic reaction speed;

1 1. Effect of temperature on enzyme reaction speed

12. Effect of pH value on enzymatic reaction speed;

13. Effect of activator on enzymatic reaction speed

14. Effect of inhibitors on enzymatic reaction speed

15. Action mechanism of enzyme

16. Active center of enzyme;

65438+

18. Factors affecting the catalytic efficiency of enzymes

19. Allosteric enzymes, isoenzymes and inducible enzymes

(vi) Vitamins and hormones

1. The concept and classification of vitamins;

2. Water-soluble vitamins

3. The relationship between water-soluble vitamins and coenzyme

4. Fat-soluble vitamins

5. Hormones

6. The concept and classification of hormones

(VII) Overview of metabolism

1. Overview of metabolism

2. Chemical reaction mechanism and metabolic types in metabolism.

3. Research methods of metabolism

(VIII) Sugar metabolism

Enzymatic degradation of 1. sugar

2. Glycolysis and regulation

3. The process of glycolysis;

4. ATP produced by glycolysis and its biological significance

5. The way of pyruvate;

6. Regulation of glycolysis

7. Tricarboxylic acid cycle

8. Oxidative decarboxylation of pyruvate;

9. Reaction process of tricarboxylic acid cycle;

10. Energy calculation in tricarboxylic acid cycle:

1 1. Biological significance of tricarboxylic acid cycle

12. anaplerotic reaction of oxaloacetic acid;

13. regulation of tricarboxylic acid cycle

14. pentose phosphate pathway

15. the process of pentose phosphate pathway;

Biological significance of pentose phosphate pathway;

Regulation of pentose phosphate pathway.

18. Sugar biosynthesis

19. Carbon fixation and calvin cycle

20. Heterogeneity of glucose;

2 1. Synthesis of glycogen and starch;

(9) Biological oxidation and oxidative phosphorylation

1. Overview of biological oxidation

2. Electron transfer chain

3. Composition and function of electron transfer chain;

4. Arrangement sequence of electron transfer chains and their transporters

5. Composition of electron transporter complex;

6. Electron transfer inhibitors

7. Oxidative phosphorylation

8. The concept of oxidative phosphorylation

9. Mechanism of oxidative phosphorylation

10. Decoupling agents and inhibitors of oxidative phosphorylation

(X) Lipid metabolism

1. Biodegradation of fat

2. Enzymatic degradation of fat

3. Degradation and transformation of glycerol

4. Oxidative decomposition of fatty acids

5. Biosynthesis of fat

6. Glycerol biosynthesis

7. Ab initio synthesis of saturated fatty acids

8. Synthesis of unsaturated fatty acids

9. Biosynthesis of triacylglycerol

10. Degradation and biosynthesis of glycerophosphate

1 1. Degradation of glycerophosphate;

12. Biosynthesis of glycerophospholipid

(Xi) protein degradation and amino acid metabolism.

Enzymatic degradation of 1. protein

2. Degradation and transformation of amino acids

3. Deamination;

4. decarboxylation;

5. The whereabouts of amino acid decomposition products, urea cycle

6. Amino acid decomposition and one carbon unit metabolism.

7. Amino acid biosynthesis

(XII) Nucleic acid degradation and nucleotide metabolism

1. Enzymatic degradation of nucleic acid

2. Enzymatic degradation of nucleotides

3. Degradation of nucleotides;

4. Degradation of purine;

5. Pyrimidine degradation

6. Nucleotide biosynthesis

7. Remedial synthesis of nucleotides

8. Ab initio biosynthesis of purine nucleotides;

9. Ab initio synthesis of pyrimidine nucleotides:

10. Biosynthesis of deoxynucleotides;

1 1. Biosynthesis of nucleoside triphosphate

(XIII) Biosynthesis of nucleic acids

1.DNA biosynthesis

2. Semi-conservative replication;

3. Reverse transcription;

4.DNA damage and repair

5.RNA biosynthesis

6.6 transcription. DNA

7. Post-transcription processing;

8.RNA replication

(XIV) Biosynthesis in protein

1. An important part of protein synthesis system.

2.mRNA and genetic code;

3 . trna;

4.rRNA and ribosome;

5. Auxiliary factors;

6. Biosynthesis in protein

7. Activation of amino acids;

8. Initiation of peptide chain synthesis;

9. Extension of peptide chain;

10. Termination and release of peptide chain synthesis

1 1. Polyribosome;

Protein biosynthesis in eukaryotic cells.

13. Processing, folding and transport of peptide chains after synthesis

(15) Regulation of metabolism

1. The relationship between metabolic pathways

2. Correlation between glucose metabolism and lipid metabolism.

3. Correlation between carbohydrate metabolism and protein metabolism.

4. Correlation between lipid metabolism and protein metabolism.

5. Interaction between nucleic acid metabolism and carbohydrate, lipid and protein metabolism.

6. Regulation of metabolism;

7. Adjustment of enzyme level;

8. Regulation of cell regionalization;

9. Regulation of energy charge on metabolism

10. Gene expression regulation

(16) Comprehensive content

1. Classical biochemical experiment and its significance;

2. Biochemistry in life;

3. Views and analysis on the frontier issues of modern biochemistry;

4. Analysis of biochemical experiment phenomenon

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