BT2402 PROTEIN ENGINEERING SYLLABUS | ANNA UNIVERSITY B.TECH BIOTECHNOLOGY 7TH SEM SYLLABUS REGULATION 2008 2011 2012-2013 BELOW IS THE ANNA UNIVERSITY SEVENTH SEMESTER B.TECH BIOTECHNOLOGY DEPARTMENT SYLLABUS, TEXTBOOKS, REFERENCE BOOKS,EXAM PORTIONS,QUESTION BANK,CLASS NOTES, IMPORTANT 2 MARKS, 8 MARKS, 16 MARKS TOPICS. IT IS APPLICABLE FOR ALL STUDENTS ADMITTED IN THE YEAR 2011 2012-2013 (ANNA UNIVERSITY CHENNAI,TRICHY,MADURAI,TIRUNELVELI,COIMBATORE), 2008 REGULATION OF ANNA UNIVERSITY CHENNAI AND STUDENTS ADMITTED IN ANNA UNIVERSITY CHENNAI DURING 2009
BT2402 PROTEIN ENGINEERING L T P C
3 0 0 3
AIM
This course aims to develop the skills of the students in the area of Protein Engineering.
This is a pre-requisite for a few elective courses offered in the subsequent semesters.
OBJECTIVES
At the end of the course, the student would have learnt structure and function of
proteins of particular importance, the student will know the production of recombinant
insulin & in general how to engineer protein to be used as therapeutics.
UNIT I BONDS AND ENERGIES IN PROTEIN MAKEUP 5
Covalent, Ionic, Hydrogen, Coordinate, hydrophobic and Vander walls interactions in
protein structure. Interaction with electromagnetic radiation (radio, micro, infrared,
visible, ultraviolet, X-ray) and elucidation of protein structure.
UNIT II AMINO ACIDS AND THEIR CHARACTERISTICS 5
Amino acids (the students should be thorough with three and single letter codes) and
their molecular properties (size, solubility, charge, pKa), Chemical reactivity in relation to
post-translational modification (involving amino, carboxyl, hydroxyl, thiol, imidazole
groups) and peptide synthesis.
UNIT III PROTEIN ARCHITECTURE 12
Primary structure: peptide mapping, peptide sequencing - automated Edman method &
mass-spec. High-throughput protein sequencing setup Secondary structure: Alpha, beta
and loop structures and methods to determine
Super-secondary structure: Alpha-turn-alpha, beta-turn-beta (hairpin), beta-sheets,
alpha-beta-alpha, topology diagrams, up and down & TIM barrel structures nucleotide
binding folds, prediction of substrate binding sites
Tertiary structure: Domains, folding, denaturation and renaturation, overview of methods
to determine 3D structures, Quaternary structure: Modular nature, formation of
complexes.
UNIT IV STRUCTURE-FUNCTION RELATIONSHIP 15
DNA-binding proteins: prokaryotic transcription factors, Helix-turn-Helix motif in DNA
binding, Trp repressor, Eucaryotic transcription factors, Zn fingers, helix-turn helix motifs
in homeodomain, Leucine zippers, Membrane proteins: General characteristics, Transmembrane
segments, prediction, bacteriorhodopsin and Photosynthetic reaction center,
Immunoglobulins: IgG Light chain and heavy chain architecture, abzymes and Enzymes:
Serine proteases, understanding catalytic design by engineering trypsin, chymotrypsin
and elastase, substrate-assisted catalysis other commercial applications.
UNIT V PROTEIN ENGINEERING 8
Advantages and purpose, overview of methods, underlying principles with specific
examples: thermal stability T4-lysozyme, recombinant insulin to reduce aggregation and
inactivation, de novo protein design.
TOTAL : 45 PERIODS
TEXT BOOKS
1. Voet D. and Voet G., “Biochemistry”, Third Edn. John Wiley and Sons, 2001
2. Branden C. and Tooze J., “Introduction to Protein Structured, Second Edition”,
Garland Publishing, NY, USA, 1999
REFERENCES
55
1. Creighton T.E. Proteins, Freeman WH, Second Edition, 1993
2. Moody P.C.E. and Wilkinson A.J. “Protein Engineering”, IRL Press, Oxford, UK,
1990.
BT2402 PROTEIN ENGINEERING L T P C
3 0 0 3
AIM
This course aims to develop the skills of the students in the area of Protein Engineering.
This is a pre-requisite for a few elective courses offered in the subsequent semesters.
OBJECTIVES
At the end of the course, the student would have learnt structure and function of
proteins of particular importance, the student will know the production of recombinant
insulin & in general how to engineer protein to be used as therapeutics.
UNIT I BONDS AND ENERGIES IN PROTEIN MAKEUP 5
Covalent, Ionic, Hydrogen, Coordinate, hydrophobic and Vander walls interactions in
protein structure. Interaction with electromagnetic radiation (radio, micro, infrared,
visible, ultraviolet, X-ray) and elucidation of protein structure.
UNIT II AMINO ACIDS AND THEIR CHARACTERISTICS 5
Amino acids (the students should be thorough with three and single letter codes) and
their molecular properties (size, solubility, charge, pKa), Chemical reactivity in relation to
post-translational modification (involving amino, carboxyl, hydroxyl, thiol, imidazole
groups) and peptide synthesis.
UNIT III PROTEIN ARCHITECTURE 12
Primary structure: peptide mapping, peptide sequencing - automated Edman method &
mass-spec. High-throughput protein sequencing setup Secondary structure: Alpha, beta
and loop structures and methods to determine
Super-secondary structure: Alpha-turn-alpha, beta-turn-beta (hairpin), beta-sheets,
alpha-beta-alpha, topology diagrams, up and down & TIM barrel structures nucleotide
binding folds, prediction of substrate binding sites
Tertiary structure: Domains, folding, denaturation and renaturation, overview of methods
to determine 3D structures, Quaternary structure: Modular nature, formation of
complexes.
UNIT IV STRUCTURE-FUNCTION RELATIONSHIP 15
DNA-binding proteins: prokaryotic transcription factors, Helix-turn-Helix motif in DNA
binding, Trp repressor, Eucaryotic transcription factors, Zn fingers, helix-turn helix motifs
in homeodomain, Leucine zippers, Membrane proteins: General characteristics, Transmembrane
segments, prediction, bacteriorhodopsin and Photosynthetic reaction center,
Immunoglobulins: IgG Light chain and heavy chain architecture, abzymes and Enzymes:
Serine proteases, understanding catalytic design by engineering trypsin, chymotrypsin
and elastase, substrate-assisted catalysis other commercial applications.
UNIT V PROTEIN ENGINEERING 8
Advantages and purpose, overview of methods, underlying principles with specific
examples: thermal stability T4-lysozyme, recombinant insulin to reduce aggregation and
inactivation, de novo protein design.
TOTAL : 45 PERIODS
TEXT BOOKS
1. Voet D. and Voet G., “Biochemistry”, Third Edn. John Wiley and Sons, 2001
2. Branden C. and Tooze J., “Introduction to Protein Structured, Second Edition”,
Garland Publishing, NY, USA, 1999
REFERENCES
55
1. Creighton T.E. Proteins, Freeman WH, Second Edition, 1993
2. Moody P.C.E. and Wilkinson A.J. “Protein Engineering”, IRL Press, Oxford, UK,
1990.
No comments:
Post a Comment
Any doubt ??? Just throw it Here...