info that i need to learn

Question 1

give me an example of a ketose

Answer 1

Fructose

Question 2

how does Cellulose structure influences its
physical properties:

Answer 2

Cellulose molecules consist of linear chains of glucose monomers linked by β-1,4-glycosidic bonds.

This linear arrangement allows for extensive hydrogen bonding between adjacent chains, forming strong microfibrils.

Question 3

how does pectin structure influences its
physical properties:

Answer 3

composed mainly of galacturonic acid units linked by α-1,4-glycosidic bonds.

Pectin contains carboxylic acid groups These acidic groups can ionize in aqueous solutions, leading to the formation of negatively charged carboxylate ions

Question 4

how does Alginate structure influences its
physical properties:

Answer 4

Alginate is composed primarily of linear chains of repeating units of β-D-mannuronic acid (M) and α-L-guluronic acid (G), linked by 1,4-glycosidic bonds.

Alginate chains can have alternating blocks of M and G residues

Question 5

how does Agar structure influences its
physical properties

Answer 5

Agar consists of two polysaccharides: agarose and agaropectin.

Question 6

what is a vitamin

Answer 6

organic compounds that are essential for various biochemical processes in the human body
They are micronutrients, meaning they are required in relatively small amounts compared to macronutrients like carbohydrates, proteins, and fats. Vitamins play crucial roles in metabolism, growth, development, and overall health.

Question 7

what is a Reducing carbohydrate

Answer 7

manipulation of dietary carbohydrate consumption with the aim of influencing physiological processes within the body. This manipulation can impact various aspects of metabolism, hormone regulation, and overall health.

Question 8

what is a FODMAP

Answer 8

stands for Fermentable Oligosaccharides, Disaccharides, Monosaccharides, and Polyols.

group of short-chain carbohydrates (sugars) and sugar alcohols found in certain foods that are poorly absorbed in the small intestine.

Question 9

the main structural features of collagen which make it a strong
structural protein

Answer 9

primarily composed of three polypeptide chains, or α chains, that coil around each other to form a triple helix

This triple helical structure is stabilized by hydrogen bonds between the amino acid residues along the chains

collagen fibers are further stabilized by covalent cross-links between adjacent collagen molecules.

Question 10

explain why phospholipids are good
membrane components.

Answer 10

Phospholipids are ideal membrane components due to their amphipathic nature, forming stable bilayers with hydrophilic heads facing outward and hydrophobic tails inward.
This arrangement provides selective permeability, allowing essential molecules to pass while maintaining cellular integrity.
Additionally, phospholipid bilayers exhibit fluidity and flexibility, enabling dynamic cellular processes and interactions.

Question 11

Give 3 roles of plasma membrane proteins

Answer 11

Transport: Many membrane proteins act as transporters or channels, facilitating the movement of ions, nutrients, and other molecules across the cell membrane.

Cell Recognition and Adhesion: Certain membrane proteins, such as glycoproteins and integrins, are involved in cell recognition and adhesion processes.

Signal Transduction: Receptor proteins located on the cell membrane serve as binding sites for signaling molecules, such as hormones

Question 12

Secondary protein structure brief note

Answer 12

involved in local folding patterns and arrangements of the polypeptide backbone

most common types of secondary structure are alpha helices and beta sheets.

Question 13

Unsaturated fatty acids

Answer 13

type of fatty acid that contain one or more carbon-carbon double bonds in their hydrocarbon chain. These double bonds introduce kinks or bends in the chain

Question 14

i. The cells in the body which store lipid.

Answer 14

adipocytes

Question 15

A structure which comprises of 3-10 amino acids.

Answer 15

peptide

Question 16

An amino acid with an acidic side chain

Answer 16

aspartic acid,

Question 17

A method used in protein purification

Answer 17

chromatography,

Question 18

A class of lipid which has roles in inflammation in the body

Answer 18

eicosanoids

Question 19

A commonly occurring dietary lipid which stabilises cell membranes.

Answer 19

phospholipids

Question 20

Describe the experimental evidence which supports the chemiosmotic hypothesis

Answer 20

Proton Gradient Formation:
-Describe early experiments demonstrating the movement of protons across membranes during electron transport

ATP Synthesis Coupled to Proton Movement
-Discuss experiments demonstrating the direct coupling between proton movement and ATP synthesis.

Question 21

List four biological processes which require ATP.

Answer 21

Cellular Respiration: ATP is essential for cellular respiration

Muscle Contraction: ATP is required for muscle contraction, allowing muscles to generate force and movement.

Active Transport: ATP is used as an energy source for active transport processes that move molecules across cell membranes against their concentration gradients.

DNA Replication and Repair: ATP is required for DNA replication and repair processes. ATP is used by enzymes involved in unwinding the DNA double helix, synthesizing new DNA strands

Question 22

What is meant by the term ‘Integration of Metabolic Pathways’? (In your answer, you should
use a diagram that provides an overview of usage of fuels OTHER THAN glucose)
[10 marks]

Answer 22

refers to the coordination and regulation of multiple metabolic pathways within an organism to maintain energy homeostasis and meet cellular energy demands.

One aspect of integration involves the utilization of fuels other than glucose, such as fatty acids and amino acids, in addition to glucose, to generate energy through cellular respiration

to answer this question:

, focusing on the citric acid cycle is an excellent approach. You can discuss how the citric acid cycle serves as a central hub for the metabolism of various fuels and the generation of key intermediates and products that are further utilized in other metabolic pathways. Highlighting the production of ATP, NADH, and FADH2, as well as the generation of precursor molecules for biosynthesis, would provide a comprehensive overview of how the citric acid cycle integrates metabolic pathways within cells. Additionally, discussing the regulation and coordination of the citric acid cycle in response to cellular energy demands and substrate availability would further emphasize its role in metabolic integration.

Question 23

Briefly describe the overall role (reaction detail not required) of the reaction(s) catalysed
by Fatty Acid Synthase

Answer 23

. The overall role of FAS is to catalyze a series of reactions that add two-carbon units from malonyl-CoA to a growing fatty acid chain, ultimately producing saturated fatty acids.

Question 24

Briefly describe the recurring cycle of 4 reactions by which cells break down activated
fatty acids.

Answer 24

Oxidation: The activated fatty acid (acyl-CoA) undergoes oxidation by the enzyme acyl-CoA dehydrogenase

Hydration: The trans-double bond is then hydrated by the enzyme enoyl-CoA hydratase

Oxidation (Second): The β-hydroxyacyl-CoA molecule undergoes a second oxidation reaction catalyzed by the enzyme β-hydroxyacyl-CoA dehydrogenase.

Thiolysis: Finally, the keto group is cleaved by the enzyme acyl-CoA acetyltransferase (thiolase), releasing a two-carbon acetyl-CoA molecule and generating a new, shorter acyl-CoA molecule,

Question 25

Discuss the following statement “Amino acid metabolism comprises transamination,
deamination, and urea cycle
stages

Answer 25

Define Each Process: Begin by providing brief definitions of transamination, deamination, and the urea cycle. Describe what each process involves and its significance in amino acid metabolism.

Discuss Transamination:
Explain how transamination involves the transfer of an amino group from one amino acid to a keto acid, forming a new amino acid and a new keto acid.
Highlight the role of transamination in the synthesis of non-essential amino acids and the interconversion of amino acids.
Provide examples of specific transamination reactions and their importance in amino acid metabolism.

Discuss Deamination:
Describe deamination as the removal of an amino group from an amino acid, resulting in the formation of ammonia and a keto acid.
Differentiate between oxidative deamination and hydrolytic deamination and explain where each process occurs in the body.
Emphasize the role of deamination in amino acid catabolism and nitrogen metabolism, particularly in the elimination of excess nitrogen as ammonia.

Discuss the Urea Cycle:
Explain the urea cycle as a series of biochemical reactions occurring primarily in the liver to detoxify ammonia by converting it into urea.
Outline the key steps of the urea cycle, including the incorporation of ammonia into carbamoyl phosphate and its conversion to urea.
Highlight the significance of the urea cycle in maintaining nitrogen balance and eliminating excess nitrogen from the body.
Interconnections and

Regulation:
Discuss the interconnections between transamination, deamination, and the urea cycle in amino acid metabolism.
Explain how these processes are interconnected and regulated to ensure proper amino acid balance and nitrogen metabolism in the body.
Highlight any regulatory mechanisms or factors that control the rates of transamination, deamination, and urea cycle activity.
Clinical Relevance (Optional):
Briefly mention any clinical conditions or diseases associated with abnormalities in amino acid metabolism, such as urea cycle disorders or defects in transaminase enzymes.
Explain how disruptions in these metabolic pathways can lead to metabolic imbalances and health problems.