Download PRACTICAL LESSON 1 SIMPLE PROTEINS. STRUCTURE AND

PRACTICAL LESSON 1
SIMPLE PROTEINS. STRUCTURE AND FUNCTION
The purpose of the lesson:
- recall structure and function of the proteins
Necessary initial level
To know:
1. classification and structure of amino acids (see Appendix I);
2. acid-base behavior of amino acids (see Appendix I);
3. interactions stabilizing of protein structure. Peptide bond (see Appendix I);
4. formation and name of di-,tri- and tetrapeptides (see Appendix I).
Key words: proteins, function of the proteins, primary structure of proteins,
secondary structure, tertiary structure, quaternary structure, classification of
proteins, protein folding, role of chaperones in protein folding, biologically
important peptides .
Content of the lesson:
1. Written control.
2. Recitation
QUESTIONS FOR PREPARATION FOR LESSON:
1. Proteins: functions of the proteins.
2. Primary structure of proteins.
3. Secondary structure.
4. Tertiary structure of proteins.
*5. Protein folding. Role of chaperones in protein folding (see Appendix I)
6. Quaternary structure.
7. Classification of proteins (see Appendix I)
*8. Other biologically important peptides.
QUESTIONS FOR WRITTEN CONTROL:
1. Draw zwitterion forms of these amino acids
a) Alanine
b)Serine
c)Glutamine
2. Why are Glu and Asp often referred to as acidic amino acids?
3. Why is Arg often referred to as a basic amino acid? Which other two amino
acids are also basic amino acids?
4. Draw structure of amino acid glycine at each pH: 6 (a), 2 (b), 11 (c). (see
Appendix III).
5. Draw the structure of amino acid valine at each pH: 6 (a), 2 (b), 11 (c).
6. Draw the positively charged, neutral, and negatively charged forms for the
amino acid phenylalanine.
7. Draw and name the tripeptide: Asp, Ala, Ser.
8. Draw and name the tripeptide: Glu, Pro, Hys.
9. Draw and name the tripeptide: Ile, Pro, Met.
10. Fill in:
The level of protein
structural organization
primary
secondary
tertiary
quaternary
Interactions stabilizing this
structure
TEST CONTROL
See Appendix II
RECOMMENDED BIBLIOGRAPHY
a) Compulsory:
1. Lectures.
2. DM Vasudevan, Sreekumari S, Kannan Vaidyanathan. (2014) Textbook of
biochemistry for medical students.7th edn. Jaypee Brothers Medical Publishers
(P) Ltd.
b) Supplementary:
1. Janice Gorzynski Smith. (2012) Principles of general, organic, and biological
chemistry. The McGraw-Hill Companies, Inc.
2. Laurence A. Moran, H. Robert Horton, K. Gray Scrimgeour, Marc D. Perry.
(2012) Principles of Biochemistry. Pearson Education, Inc.
3. Lehninger A., David L. Nelson, Michael M. Cox. (2008) Lehninger Principles
of Biochemistry. 5th edn. W.H.Freeman and company, New York.
4. Mary K. Campbell, Shawn O. Farrell Biochemistry. (2012) Biochemistry. 7th
edn. Brooks/Cole, Cengage Learning.
5. Pamela C. Champe, Richard A. Harvey, Denise R. Ferrier. (2004) Lippincott’s
Illustrated Reviews: Biochemistry. Lippincott Williams & Wilkins
6. Reginald H. Garrett, Charles M. Grisham. (2010) Biochemistry. Brooks/Cole,
Cengage Learning.
7. Robert K. Murray, David A Bender, Kathleen M. Botham, Peter J. Kennelly,
Victor W. Rodwell, P. Anthony Weil. (2009) Harper's Illustrated Biochemistry.
28th edn. The McGraw-Hill Companies, Inc.