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CSIR Mock Paper 5
CSIR Mock Paper 5
CSIR Mock Paper 5
Part A- 1-20
Part B- 21 to 70
Part C- 71 to 145 Mock Test
CSIR-NET-JRF- Life Science
MCQ Type
Total Time- 3 h
Part- A shall carry 20 questions and candidates required to answer any 15 questions.
Part- B shall contain 50 Multiple Choice Questions (MCQs) and required to answer any 35 questions.
Part- C contains 75 questions and candidates required to answer any 25 questions. Each question of
Part- C carries four marks. There will be negative marking @25% for each wrong answer. Answer Key will
be provided along with the mock test. You can check your preparation after giving each test. The total
time allotted for the exam is 3 hrs.
Part A
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Part B
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Part C
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BIOLOGY TEST
Time— 170 minutes
Questions 130-132 refer to the following. Questions 133-136 refer to the following functions.
194 Questions
(A) Actin (A) Respiration
Directions: Each of the questions or incomplete statements below(B)
(B) Tubulin Support by five suggested answers or
is followed
completions. Select the one that is best in each case and then completelyLocomotion
(C) Calmodulin (C) fill in the corresponding space on the
(D) sheet.
answer Fibronectin (D) Feeding
(E) Troponin (E) Excretion
130.
1. Bipolar-filament-forming protein
Which of the following pairs that bindswould
of molecules and 133.
2. Radula
Proteinsofdestined
molluscsto be secreted move through
hydrolyzes GTP
form hydrogen bonds? the secretory pathway in which of the following
orders? of sponges
134. Spicules
131. Major cytoskeletal protein in microvilli, filopodia,
contractile rings, and growth cones (A) Smooth ER Æ Golgi transport vesicle Æ
135. Nematocysts of cnidarians
Golgi cisternae Æ secretory vesicle Æ
132. Calcium-binding switch protein in vertebrate cell surface
skeletal muscle fibers Æ Golgi transport vesicle Æ
136. Tracheae ofER
(B) Rough insects
Golgi cisternae Æ secretory vesicle Æ
cell surface
(C) Golgi cisternae Æ ER transport vesicle Æ
smooth ER Æ secretory vesicle Æ
cell surface
(D) Golgi cisternae Æ ER transport vesicle Æ
rough ER Æ secretory vesicle Æ
cell surface
(E) Rough ER Æ smooth ER Æ Golgi transport
vesicle Æ Golgi cisternae Æ secretory
vesicle Æ cell surface
(A) I only 3. Stabilization of the unique coiled structure
(B) III only of an alpha helix in a protein is primarily
(C) IV only attributed to
(D) I and II only
(E) II, III, and IV (A) hydrogen bonding between the peptide
backbone atoms
(B) disulfide bridges between cysteine side
chains
(C) carbohydrate moieties attached to polar
amino acids
(D) peptide linkages that covalently bond amino
acids
(E) an abundance of amino acids with electrically
charged side chains
137.
1. A groupofofthe
Which potentially
followinginterbreeding individuals
pairs of molecules would 2. Proteins destined to be secreted move through
present at the same
form hydrogen bonds? location the secretory pathway in which of the following
orders?
138. A group of potentially interacting species present
at the same location (A) Smooth ER Æ Golgi transport vesicle Æ
Golgi cisternae Æ secretory vesicle Æ
139. A large geographical area characterized by its cell surface
dominant form of vegetation (B) Rough ER Æ Golgi transport vesicle Æ
Golgi cisternae Æ secretory vesicle Æ
140. All organisms and their nonliving environment
cell surface
present at the same location
(C) Golgi cisternae Æ ER transport vesicle Æ
smooth ER Æ secretory vesicle Æ
141. Location
cellof RNA primer
surface
(D) Golgi cisternae Æ ER transport vesicle Æ
142. Location of DNA
rough ER Æpolymerase
secretory vesicle Æ
cell surface
143. Location of DNA with a free 3¢ OH
(E) Rough ER Æ smooth ER Æ Golgi transport
vesicle Æ Golgi cisternae Æ secretory
vesicle Æ cell surface
(A) I only 3. Stabilization of the unique coiled structure
(B) III only of an alpha helix in a protein is primarily
(C) IV only attributed to
(D) I and II only
(E) II, III, and IV (A) hydrogen bonding between the peptide
backbone atoms
(B) disulfide bridges between cysteine side
chains
(C) carbohydrate moieties attached to polar
amino acids
(D) peptide linkages that covalently bond amino
acids
(E) an abundance of amino acids with electrically
charged side chains