COLLEGE OF ENGINEERING AND TECHNOLOGY
A SCHOOL OF BIOENGINEERING, DEPARTMENT OF BIOTECHNOLOGY
B. Tech. Biotechnology,
B. Tech. Biotechnology (Splzn. – Regenerative Medicine) and
B. Tech. Biotechnology (Splzn. – Genetic Engg.) Programs
ACADEMIC YEAR 2025-26 ODD SEMESTER
Continuous Learning Assessment Test I (FTII)
Reg. No. R A
Course Code: 21BTC303T Course Title: Protein Engineering
Sem & Year: V/III Date:08/09/2025 Duration: 50 Minutes Max. Marks: 25
Course Outcomes (COs) Program Outcomes (POs) PSOs
1 2 3 4 5 6 7 8 9 10 11 1 1 2 3
2
Outline proteins and its - 2 - - - - - - - - - - 3 -
properties at the elemental, -
CO-1:
molecular and structural
levels
Q. No. PART A- Answer All Questions Marks BL CO Marks PO(s)/
Scored PSO
1. Provide the chemical structure and discuss 5 L1 1
about basic and acidic amino acids and their
significance in protein function and protein
folding (Discussion about charged amino
acids with structure, ionic interactions in
tertiary protein structure, role of charged
amino acids in protein function).
2. Peptide conformation is defined by dihedral 5 L3 1
angles. Explain with neat sketch. (Phi, Phsi
and Omega angles explained with diagram)
3. R-side chains defines the tertiary interactions 5 L2 1
of protein molecules. Explain with
appropriate sketch (Tertiary protein structure
and bonds involved in it)
Q. No. PART B- Answer Any 1
4. Elaborate on the secondary structure 10 L2 1
stabilized by main chain hydrogen bonding
(n, n+4) parallel to its axis (alpha Helical
structure, unusual alpha helix, helix
favouring and helix breaking amino acids,
helical angles in Ramachandran Plot)
5. Protein folding occurs in ATP-driven 10 L2 1
machine when the temperature of a system is
high where proteins are denatured. Elaborate
on protein folding process with neat sketch
(GroEL and GroES protein folding system in
[Link])
COLLEGE OF ENGINEERING AND TECHNOLOGY
B SCHOOL OF BIOENGINEERING, DEPARTMENT OF BIOTECHNOLOGY
B. Tech. Biotechnology,
B. Tech. Biotechnology (Splzn. – Regenerative Medicine) and
B. Tech. Biotechnology (Splzn. – Genetic Engg.) Programs
ACADEMIC YEAR 2025-26 ODD SEMESTER
Continuous Learning Assessment Test I (FTII)
Reg. No. R A
Course Code: 21BTC303T Course Title: Protein Engineering
Sem & Year: V/III Date:08/09/2025 Duration: 50 Minutes Max. Marks: 25
Course Outcomes (COs) Program Outcomes (POs) PSOs
1 2 3 4 5 6 7 8 9 10 11 1 1 2 3
2
Outline proteins and its - 2 - - - - - - - - - - 3 -
properties at the elemental, -
CO-1:
molecular and structural
levels
Q. No. PART A- Answer All Questions Marks BL CO Marks PO(s)/
Scored PSO
1. The core of a globular protein is hydrophobic 5 L1 1
in nature. Discuss about the R-side chains of
amino acids that contribute to hydrophobicity
with appropriate chemical structures
(aliphatic and aromatic amino acids and their
R-Side chains contribution to hydrophobic
interactions in the tertiary protein structure)
2. A nascent polypeptide assumes biologically 5 L3 1
active confirmation through different
chemical bonds. Explain with appropriate
sketch (Explain different covalent and non-
covalent bonds present in tertiary structure).
3. Discuss the conclusions of ANFINSEN 5 L2 1
experiment with appropriate sketch (All the
information necessary for protein folding is
contained in the amino acid sequence of
protein)
Q. No. PART B- Answer Any 1
4. A group of amino acids that have a local 10 L2 1
arrangement or inter arrangement where the
hydrogen bonds are perpendicular to the
main chain. Provide a neat sketch and explain
its attributes in detail (Discussion about beta
pleated, parallel and antiparallel sheet
secondary structure, its function in protein
compaction, examples of proteins with
parallel and antiparallel secondary structures)
5. Show that the conserved region of a protein 10 L2 1
that appears in the bottom left-hand quadrant
of the Ramachandran plot is a typical
secondary structure. Elaborate in detail with
appropriate sketch (Alpha Helix structural
features and main chain hydrogen bonding,
unusal alpha helix, phi and Psi angles of
alpha Helix, Ramchandran Plot showing
allowed angles for alpha helix in bottom left-
hand quadrant)
COLLEGE OF ENGINEERING AND TECHNOLOGY
C SCHOOL OF BIOENGINEERING, DEPARTMENT OF BIOTECHNOLOGY
B. Tech. Biotechnology,
B. Tech. Biotechnology (Splzn. – Regenerative Medicine) and
B. Tech. Biotechnology (Splzn. – Genetic Engg.) Programs
ACADEMIC YEAR 2025-26 ODD SEMESTER
Continuous Learning Assessment Test I (FTII)
Reg. No. R A
Course Code: 21BTC303T Course Title: Protein Engineering
Sem & Year: V/III Date:08/09/2025 Duration: 50 Minutes Max. Marks: 25
Course Outcomes (COs) Program Outcomes (POs) PSOs
1 2 3 4 5 6 7 8 9 10 11 1 1 2 3
2
Outline proteins and its - 2 - - - - - - - - - - 3 -
properties at the elemental, -
CO-1:
molecular and structural
levels
Q. No. PART A- Answer All Questions Marks BL CO Marks PO(s)/
Scored PSO
1. The surface of protein molecules are rich in 5 L1 1
hydrophilic amino acids. List the hydrophilic
amino acids with chemical structure and
highlight the hydrophilic R-side chains
(Discussion about hydrophilic amino acids,
R-side chains of hydrophilic aminoacids in
ligand binding and protein functions).
2. Secondary structure becomes super 5 L3 1
secondary structure due to
intervening/irregularly structured peptide
sequences. Explain with appropriate
example and structure of super secondary
structure and their significance in protein
conformation and function (Different types
of Motifs with apprpirate sketch and their
occurrence in different class of proteins)
3. PDI promotes protein folding through correct 5 L2 1
covalent bond formation. Explain (Role of
protein disulphide isomerase in protein
folding)
Q. No. PART B- Answer Any 1
4. Elaborate on motifs present in (a) calcium 10 L2 1
binding proteins and (b) Staphylococcus
nuclease.
EF Hand Motif and Greek Key Motif
5. Show that the conserved region of a protein 10 L2 1
that appears in the top left-hand quadrant of
the Ramachandran plot is a typical secondary
structure. Elaborate in detail with appropriate
sketch (Beta pleated sheet, phi and Psi angles
of beta pleated sheet, parallal and antiparallel
strucutures, Ramachandran Plot)
COLLEGE OF ENGINEERING AND TECHNOLOGY
D SCHOOL OF BIOENGINEERING, DEPARTMENT OF BIOTECHNOLOGY
B. Tech. Biotechnology,
B. Tech. Biotechnology (Splzn. – Regenerative Medicine) and
B. Tech. Biotechnology (Splzn. – Genetic Engg.) Programs
ACADEMIC YEAR 2025-26 ODD SEMESTER
Continuous Learning Assessment Test I (FTII)
Reg. No. R A
Course Code: 21BTC303T Course Title: Protein Engineering
Sem & Year: V/III Date:08/09/2025 Duration: 50 Minutes Max. Marks: 25
Course Outcomes (COs) Program Outcomes (POs) PSOs
1 2 3 4 5 6 7 8 9 10 11 1 1 2 3
2
Outline proteins and its - 2 - - - - - - - - - - 3 -
properties at the elemental, -
CO-1:
molecular and structural
levels
Q. No. PART A- Answer All Questions Marks BL CO Marks PO(s)/
Scored PSO
1. What are essential, non-essential and 5 L1 1
uncommon amino acids? Explain by
appropriately citing amino acids. Identify the
occurrence of uncommon amino acids in
specific protein molecules. (Essential, non
essential amino acids, list four uncommon
amino acids in specific proteins)
2. Discuss the significance of certain peptide 5 L3 1
regions in the enzyme active site/protein
surface that are variable in length and shape
(Loop Regions)
3. Differentiate molten globule intermediate 5 L2 1
from fully folded tertiary structure (Molten
globule is intermediate in protein folding and
difference with tertiary strucuture)
Q. No. PART B- Answer Any 1
4. Folding of newly made polypeptide into fully 10 L2 1
folded structure requires sequence of
stabilizing bonds. Elaborate with appropriate
sketch describing different levels of protein
structure (Primary, secondary, tertiary and
quarternary structures. Covalent and non
covalent bonds in protein structure with 3D
protein structure diagram)
5. Elaborate the mechanism of [Link] HSP60 10 L2 1
and HSP10 assisted protein folding (GroEL
and GroES chaperons in protein folding)