2024 ASRJC H2 Bio P1 QP

ASRJC BIOLOGY DEPT 9744/2024/J2PRELIMS/P1 [Turn over 2024 JC2 PRELIMINARY EXAMINATIONS BIOLOGY 9744/01 PAPER 1 13 SEPTEMBER 2024 MULTIPLE CHOICE FRIDAY 1 HOUR Additional Materials: Multiple Choice Answer Sheet READ THESE INSTRUCTIONS FIRST Write in soft pencil. Do not use staples, paper clips, highlighters, glue or correction fluid. Write your name, class and identification number on the MCQ Answer Sheet. There are thirty questions on this paper. Answer all questions. For each question there are four possible answers A, B, C and D. Choose the one you consider correct and record your choice in soft pencil on the separate Answer Sheet. Each correct answer will score one mark. A mark will not be deducted for a wrong answer. Any rough working should be done in this booklet. The use of scientific calculators is expected, where appropriate. This document consists of 23 printed pages and 1 blank page. H2 ANDERSON SERANGOON JUNIOR COLLEGE HIGHER 2

2 ASRJC BIOLOGY DEPT 9744//2024/J2PRELIMS/P1 1 What can be found in both eukaryotic and prokaryotic cells? 1 circular DNA 2 lipids 3 ribose 4 peptidoglycan cell wall A 1, 2 and 3 B 1, 2 and 4 C 2 and 3 D 3 and 4 2 Hydroxyproline is a component of collagen. The graph shows the effect of temperature on the triple helix structure of collagen with and without hydroxyproline. The y-axis of the graph indicates the percentage of intact triple helix structure in a sample of collagen. Which statement(s) explain(s) the importance of hydroxyproline in the structure of collagen? 1 Presence of hydroxyproline increases thermal stability of collagen as hydroxyproline facilitates formation of covalent cross-links within each triple helix structure. 2 At higher temperatures, collagen with hydroxyproline results in less triple helices present than collagen without hydroxyproline. 3 Hydroxyproline contributes to the extensive hydrogen bonds that hold the polypeptide chains of each triple helix structure. A 1 only B 3 only C 1 and 2 D 2 and 3 collagen without hydroxyproline collagen with hydroxyproline temperature / °C triple helix structure / % key

3 ASRJC BIOLOGY DEPT 9744//2024/J2PRELIMS/P1