Learning outcomes Flashcards

1
Q

Define aetiology and pathogenesis

A
Aetiology = cause of disease
Pathogenesis = how it develops
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Define symptoms and signs

A
Symptom = what patient feels
Sign = our (doctors) observations
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

Define diagnosis and prognosis

A
Diagnosis =  Defined abnormalities 
Prognosis = Predicted outcome
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Define natural history and classification of disease

A

Natural history = course of disease without treatment
Classification of disease:
1. Inflammation - Response of living tissue when injured
2. Circulatory disturbances - Abnormalities of blood components, vessels or flow.
3. Disorders of growth - Abnormal cell growth (types - maturation, differentiation, control, quantity)
4. Degenerative disease - Abnormalities of tissue and organs
5. Developmental - Abnormalities in the genetic information of gametes or embryos (gametogenesis and embryogenesis)
6. Unnatural - Traumatic (accident) and Iatrogenic (as a result of treatment)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Understand the general organisation of the body systems

A

The body is made up of cells. A group of cells that share the same characteristics or specialisation and perform the same function are called tissues. A collection of tissues usually of different types that synchronise to perform a more complex function is called an organ. When multiple organs work in synchrony this is known as a organ system. Multiple organ systems working together creates an organism.

Organ systems are designed to support the production of energy. The study of how the systems function and work together is called physiology. Each system has a role in maintaining life. Therefore their role can be shown in relation to the equation of life. Nutrients + O2 = Energy (ATP) + waste (incl. CO2)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Be able to outline the role of each major system in maintaining health and optimal
homeostasis

A

Cardiovascular System = Delivers O2 and nutrients to cells, removes waste from cells
Respiratory System = Acquires O2, disposes of CO2
Gastrointestinal System = Acquires nutrients, disposes of waste (faeces)
Renal System = Disposes of waste (urine)
Musculoskeletal System = Sources nutrients (allows you to find and eat food), removes us from danger, protects from threat (allowing us to continue living and eating).
Immune System = Protects us from infection (conserving energy? and allowing other systems to function)
Nervous System = Coordinates other systems
Endocrine System = Coordinates other systems, major role in allowing cellular access to nutrients that have been absorbed. (Takes nutrients from blood to cells)
Reproductive System = Ensures continuation of life

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Define the term homeostasis

A

The prevention of the disturbance in the system is known as homeostasis.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Explain the importance of maintaining constancy of the internal environment

A

Our bodies are not very tolerant to change and therefore are constantly monitoring their internal state and responding to any threat to a change in there ‘similar internal conditions’.
Failure to adequately correct imbalances results in illness and disease, or pathology (Latin for suffering).
For example if you ate a sugary donut, glucose is absorbed across intestinal tract and the hormone insulin is released to remove glucose from the blood almost as fast as it enters to prevent blood glucose levels from rocketing.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Describe the principles behind negative feedback control systems

A

This mechanism is called “Negative” feedback because the condition that triggered the homeostatic response becomes switched off/removed by that response.
The size of the response is proportional to the size of the disturbance.
When a condition that is homeostatically regulated (e.g. body temperature), is sensed to have shifted from the normal range, a signal (usually nervous or endocrine), is generated that produces a response (e.g. shivering or sweating), that corrects the original disturbance and brings the regulated condition back within the normal range
Characteristics: . There is oscillation around the set point. Restores the regulated condition after its initial disturbance, but cannot prevent it happening

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Explain what is meant by feed forward control

A

Feed forward systems are more sophisticated and can, to some extent, predict and prevent change. Feed forward systems contain additional receptors that permit system to anticipate change and therefore activate response earlier.
i.e. when you are thirsty the kidney detects the increased body fluid concentration and pre-empts a state of dehydration. It responds by producing smaller volumes of urine, and a more concentrated form of urine, thus conserving water.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Illustrate the concept of homeostasis by outlining daily water balance in man

A

When a person is working outside on a hot dry day there body looses water through evaporation. This results in the body fluid becoming more concentration, Internal receptors sense change in this internal condition and simulate the thirst pathway. The person seeks out water and drinks. This process demonstrates both negative feedback and feedforward pathways. The water balance of a person is homeostatically controlled and therefore when the concentration changes the body responses by releasing signals which lead to the return to normal concentration.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Identify the different body fluid compartments

A

Water is stored in 3 different compartments.

  1. Intracellular fluid
  2. Interstitial fluid (fluid between cells)
  3. Plasma (fluid component of blood)

The plasma and interstitial fluid make up what is known as the extracellular fluid.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Explain the importance of the nature of the barriers which separate the body
compartments

A

Natural barrier are important in maintaining concentration gradients within the body. The composition of plasma and interstitial fluid is very similar because the natural barrier that separates them is not very selective. However the composition of the extracellular fluid and the intercellular fluid is significantly different because the cell membrane is very selectively permeable. Life can only be maintained while the composition of these different fluid compartments is maintained therefore the natural barriers are extremely important.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Define the dilution principle

A

The dilution principles states that v = m/c

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Describe the use of the dilution principle in the measurement of body fluid
compartments

A

Plasma is the only fluid compartment that we can access. Therefore:

Measuring the plasma volume: Add a dye or label that cannot cross the capillary wall. Let dye of label distribute then measure the concentration and calculate the volume using the dilution principle.

Measuring the extracellular volume: Add a molecule that can cross the capillary wall but not the cell wall. Let it distribute then measure the concentration and calculate the volume using the dilution principle.

measuring the total body fluid volume: Add a substance that can cross the capillary wall and cell wall i.e. heavy water . Let dye of label distribute then measure the concentration and calculate the volume using the dilution principle.

Measuring the interstitial fluid volume: Extracellular Fluid - Plasma Volume

Measuring the intracellular fluid: Total Body Water -Extracellular Fluid

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Define metabolism catabolism and anabolism, and describe, in outline, how they are
interdependent

A

Metabolism describes the chemical processes of a living organisms by which the energy stored in food is used for tissue growth and energy production.
Metabolism can be split into two pathways. Anabolic and catabolic.
In the catabolic pathways food molecules are broken down and oxidised to form more simple molecules. Some of energy released from this is lost in heat (2nd law of thermodynamics) however most of it is used to fed the anabolic pathways.
In the anabolic pathway small molecules are combined to form more complex molecules.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Describe, in general terms, the structures and contributions to metabolic flow of ATP,
ADP, NADP, NAD, FAD

A

These are Intermediary Metabolites. These are used to store energy and therefore allow thermodynamically unfavourable reactions to proceed (anabolic pathways).

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Compare, in outline, the processes of substrate-level and oxidative phosphorylation

A

????

Phosphorylation and dephosphorylation is the process by which energy can be stored or released. ATP to ADP + Pi.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

Define the major elements used to construct human biomolecules

A

????

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

State the importance of chemical functional groups and molecular configuration and
conformation in determining biomolecular function

A

Functional groups determine the function of a molecule. Molecules often contain functional groups which are groups of elements bonded to a carbon atoms. Example of function groups include, Hydroxyl group (-OH), aldehyde group (-CHO ) and the Keto group (R2C=O). Biochemical molecules can be defined by these functional groups.
The function of molecules is also determined by their conformation. Molecules can be cis or trans. The orientation of this can completely change there function.
The polarity of a molecule can also determine its function. Polarity is the distribution of electrons within a bond.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

List and give examples of the five kinds of chemical reaction occurring in living
organisms

A
  1. Redox reactions. i.e. glucose to pyruvate
  2. Making and breaking C-C bonds. i.e. Cleavage of glucose in glycolysis
  3. Internal rearrangements. i.e. The rearrangement of the conformation of G6P occurs before the sugar is split in glycolysis
  4. Group transfers. i.e. In an enzyme catalysed reaction, a phosphoryl group (PO32-) is transferred from ATP to F6P as part of glycolysis.
  5. Condensation and hydrolysis reactions. i.e. construction of a carbohydrate, sucrose.
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

Describe the general structures of proteins, nucleic acids, polysaccharides and lipids

A

Proteins are long chains of amino acids. Nucleic acids form the core structure of DNA and RNA. Nucleic acids are polymers composed of nucleotide monomers. A polysaccharides (complex carbohydrates) such as starch or glycogen are composed of many individual monosaccharide molecules e.g. glucose. Lipids consist of fatty acids. There are three classes of lipids: 1. Triacylglycerides 2. Phospholipids 3. Sterols

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

Describe the structures present in all cell types

A

All cells have a cell membrane and cell organelles. Cell organelles are the “machinery” of the cell. All substances entering or leaving the cell must cross the cell membrane

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

Define the roles of eukaryotic animal cell organelles: nucleus, nucleolus, endoplasmic
reticulum, ribosome, Golgi apparatus, lysosome, peroxisome, mitochondrion,
flagellum, cilium

A

Nucleus:
Contains DNA, nucleoprotein and some RNA
Nucleoli are sites of ribosomal RNA synthesis and ribosomal assembly. The nucleus is enclosed in the nuclear membrane which, like all biological membranes, is a phospholipid bilayer. It is closely associated with the Rough Endoplasmic Reticulum

Endoplasmic reticulum
Membrane bound organelles. Endoplasmic reticulum comes in rough (RER) and smooth (SER) varieties
RER has ribosomes attached giving it the “rough” appearance. RER modifies proteins. SER has no ribosomes attached and is mainly associated with lipid and steroid hormone production and metabolism of toxins

Ribosomes
Ribosomes synthesise proteins.

Golgi Apparatus
Golgi Apparatus packages up protein in preparation for transport out of the cell.

Lysosome
Enzymes are one form of protein packaged by the golgi apparatus. Enzymes catalyse reactions in cells but need to be stored until needed. Lysosomes are membrane bound vesicles containing enzymes – they separate enzymes from the rest of the cell. Used in autophagy (digestion of cells own materials) or digestion of engulfed particles (e.g. bacteria). Peroxisome are similar.

Mitochondria
Mitochondria are also organelles bound by a phospholipid bilayer. Outer membrane contains pores. Inner membrane has cristae (folds). Matrix contains most of the enzymes required for metabolising food molecules (e.g. Krebs cycle)

Some cells have surface projections supported by the cytoskeleton i.e. Cilia and eukaryotic flagella are made of microtubules. Cilia—short, usually many present, move with stiff power stroke and flexible recovery stroke. Flagella—longer, usually one or two present, movement is snakelike

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

Correlate organelle structure with function

A

???

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

Describe the structure and function of the eukaryotic plasma membrane.

A

The cell membrane (Sometimes called the plasma membrane or plasmalemma) comprises of a double layer of lipid with attached phosphate groups. This double layer of lipids is known as the phospholipid bilayer (See Forces Across Membranes for more detail). Embedded in the membrane are proteins which act as receptors to detect chemical messengers and signalling molecules in the fluid surrounding cells (extracellular fluid)
The phospholipid bilayer forms a selective barrier, being choosy about what it allows to cross in or out of the cell

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

Define the role of the cytoskeleton

A

Supports and maintains cell shape
Holds organelles in position
Helps move organelles around the cell
It is compromised of one of three forms of protein: microfilaments, intermediate filaments, microtubules.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
28
Q

Describe the interactions between water molecules and solutes that determine solubility.

A
When charged (polar) particles are dissolved in water the water forms a “screen” around them. 
i.e. When sodium chloride (common salt) is dissolved in water, the water forms ‘screens’ around each ion keeping the Na+ and Cl- ions in solution once dissolved. (Preventing them from reacting and forming sodium chloride)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
29
Q

Define the term ‘pH’ and derive an expression that relates the degree of proton
dissociation of a weak acid to its ionisation constant and the pH

A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
30
Q

Describe what is meant by the term ‘buffer’

A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
31
Q

Describe the basic structure of membranes

A

Membranes are composed of a phospholipid bilayer (with hydrophilic head and hydrophobic tails) and proteins and or carbohydrates. Proteins can be peripheral or integral. The cell membrane is selectively permeable. This permeability may vary over time. The membrane is dynamic, continually being formed and dismantled. Membranes are flexible and can expand though they will burst if they expand too much. Membranes are excellent insulators against electrical charge.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
32
Q

Describe the functions of the cell membrane

A

Form a natural barrier between the intracellular and extracellular environments. The proteins embedded in the cell membrane are used as receptors, for transport (transporter and channel proteins), as enzymes, for maintenance of cell structure (anchorage) and for communication.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
33
Q

Define what is meant by diffusion across membranes

A

Diffusion is the process by which a gas or substance in solution expands to fill all the available volume. Therefore molecules spread from regions of high concentration to regions of low concentration, until the concentration is uniform throughout the volume

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
34
Q

List the factors which favour diffusion through the lipid bilayer

A

Small, Uncharged and Lipophilic (hydrophobic)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
35
Q

Describe the different general types of membrane proteins and their functions

A

Peripheral proteins – associated only with the phosphate head of the lipid bi-layer and do not penetrate the hydrophobic core
Integral proteins – span the hydrophobic core of the lipid bi-layer

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
36
Q

Define electrochemical gradients

A

Electrochemical gradient is the net effect of the electrical and concentration gradient which ultimately drives the direction of passive movement.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
37
Q

Explain what is meant by carrier mediated transport systems

A

Molecules too big to move through channel proteins use carrier-mediated transport proteins or “transporters”.
These proteins have binding sites for the solutes they transport such as glucose. When they bind the solute, the transporter undergoes a change in shape which exposes the binding site on the other side of the membrane. The solute moves away from the transporter and the transporter returns to its original configuration.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
38
Q

Explain the difference between osmolarity and tonicity

A

Osmolarity describes total number of particles in solution

Tonicity describes the number of non-penetrating particles in solution.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
39
Q

Understand the physiological significance of osmolarity vs tonicity

A
Almost 20% hospital patients suffer complications due to inappropriate fluid administration. Some of these people die.
Intravascular haemolysis (cells bursting) can kill. This is because Lysed (burst) cells introduce protein to ISF, increasing tonicity of ECF in an uncontrolled manner, making management very complicated.
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
40
Q

Explain the difference between an isosmotic solution and an isotonic solution

A

An isosmotic solution has the same total number of solute particles as normal ECF (plasma).
An isotonic solution has the same number of non-penetrating solute particles as normal ECF (plasma).

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
41
Q

Describe the processes of endocytosis and exocytosis

A

These are mechanisms for moving macromolecules across membranes without disrupting them.
In endocytosis, there is invagination of the cell membrane to form a vesicle which eventually disintegrates on the cytoplasmic (inside) surface of the membrane, releasing contents which then migrate within the cell to their destination.
Endocytosis of membrane receptors is a common mechanism of terminating signals from extracellular ligands

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
42
Q

List the major cells involved in the innate and adaptive immune response systems.

A

Innate: Epithelial barriers, phagocytes, dendritic cells, complement, natural killer cells, Eosinophils, mast cells, Basophils, cytokines.
Adaptive : B and T lymphocytes, Effector T cells

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
43
Q

Describe the main role of the innate immune system

A

Distinguishes between human cells and pathogens, but not between different types of pathogen
Fast and immediate: first to come into play
No memory: will produce the same response no matter what it is or whether this pathogen has invaded before.

44
Q

Describe the functions of natural killer cells

A

-

45
Q

Describe the process of phagocytosis and intracellular killing

A

Phagocytes: are the cells of the immune system that track down, engulf and destroy bacteria, other pathogens as well as own damaged or dead cells.
Movement of the phagocyte toward the microbe

Phagocytosis looks like this:
Attachment of microbes to phagocyte surface
Endocytosis of microbe and formation of phagosome
Fusion of phagosome with lysosome
Killing of microbe through digestion by enzymes
Discharge of waste materials

46
Q

Define the primary and secondary lymphoid organs and their functions.

A

Primary: Bone Marrow and thymus. Places where blood cells are produced and receive their ‘early training’ (acquire ability to interact with antigens)

Secondary: lymph nodes, tonsils, spleen. These are sites of Lymphocyte activation by antigens and the development of adaptive immune response to Antigens by T and B cells.

47
Q

Illustrate antibody the structure and function of antibody.

A

Antibodies: are proteins that are produced as an immune response against antigens
Different antigens induce the production of different antibodies

48
Q

Describe how antigen processing cells and T-lymphocytes interact

A

-

49
Q

Describe the role of T-helper 1 and T helper 2 lymphocytes in controlling the immune
response

A
  • They cannot kill infected cells or pathogens

- They activate and direct other immune cells

50
Q

Briefly describe the complement system and its main function

A

Complement system consists of more than 30 proteins/factors that are found in the plasms, present in an inactive form
They are activated in a cascade –like format
activation of the complement in fact takes place on the surface of the target cells

51
Q

Describe the role of cytokines as chemical messengers within the immune system

A

Small proteins – secreted by both immune and some nonimmune cells in response to stimulus.
They communicate with other cells bind to specific receptors on these cells producing a signalling molecules that lead to many biological effects in these cells.

52
Q

Know the average circulating volume in a typical adult male

A

5 litres

53
Q

List the functions of blood

A
  1. Carriage of physiologically active compounds i.e.
  2. hormones (carried in the plasma)
  3. Clotting (platelets)
  4. Defence (white blood cells)
  5. Carriage of gas (red blood cells)
  6. Thermoregulation
  7. Maintenance of ECF pH
54
Q

Describe the composition of plasma

A

95% is water
The composition of the plasma is normally kept within strict limits. (if test results showed that the levels of a hormone etc were at an unusual level that suggests that there is something going wrong with the organ or system associated with that hormone)

55
Q

Name the plasma proteins and describe their functions

A

Albumin – Creates oncotic pressure and circulates steroid hormones and fat soluble vitamins (lipophilic). These use albumin as a transporter because they don’t easily dissolve in water. Albumin makes up about 60% of the plasma proteins)

2) Globulin - Subdivided into , ß,  globulins. Globulins make up 38% of plasma proteins. Alpha and Beta globulins act in a very similar way to albumin (transporter proteins for steroid hormones and flat soluble vitamins). Gamma globulins act as antibodies (important role in immune system).
3) Fibrinogen and other clotting factors. Make up 2% of the plasma proteins

56
Q

Define the term oncotic pressure and describe the factors responsible for generation

A

Movement of water from a higher concentration in the interstitial fluid into the lower water concentration (due to the presence of proteins ) in the plasma.

57
Q

Know the normal lifespan of red blood cell and platelets in the circulation

A

Blood cells: 120 day lifespan

Platelets: Life span 10 days

58
Q

Describe the function of the red blood cell

A

Transport oxygen around the body.

59
Q

Describe the function of erythropoietin, where it is synthesised and the factors which
may increase secretion

A

Erythropoietin is a hormone that controls and accelerates erythropoiesis (while in the bone marrow). 85% of erythropoietin is secretion in the kidney. The other 15% is secreted in the liver. Secretion of erythropoietin is enhanced when oxygen delivery to kidneys is reduced (hypoxia) i.e. when there is a low level of oxygen in the blood

60
Q

Name the five main types of white blood cells

A

Monocytes, Neutrophils, Basophils, Eosinophils and lymphocytes.

61
Q

Be able to classify the different types of blood cells

A

White blood cells: Monocytes, Neutrophils, Basophils, Eosinophils and lymphocytes
Red blood cells: Erythrocytes
Myeloid cells: Erythrocytes, Platelets, Monocytes, Neutrophils, Basophils and Eosinophils

62
Q

Appreciate the difference between a monocyte and a macrophage

A

5% circulating cells are monocytes. After 72 hours they migrate to connective tissue where they become macrophages and live for 3 months (important cells that carry out phagocytosis)

63
Q

Know the unique function of platelets

A

Membrane bound cell fragments. Adhere to damaged vessel walls and exposed connective tissue to mediate blood clotting. Forming the foundation of a blood clot. The platelets are not part of the clotting process, but they form the foundation that allows the clotting process to proceed.

64
Q

Outline the role of thrombopoietin in platelet formation

A

Formation of platelets is governed by Thrombopoietin

65
Q

Define what is meant by haematocrit

A

The haematocrit is a procedure used to determine the red blood cell volume. Normally red blood cells account for 40 – 50 % of the blood sample. Whether this is the case of not can be seen when a blood sample is put into a centrifuge.

66
Q

State the normal value for haematocrit and appreciate how this may change in certain
circumstances

A

Normally 40 – 50 %.
In dehydration that % will increase. The % will also increase if the patient has high levels of erythropoietin. Erythropoietin is an drug that can be taken illegally as a way of doping in sport. A hematocrit can show if this is the case.

67
Q

Define what is meant by blood viscosity

A

How thick/sticky blood is compared to water. The plasma - x 1.8 thicker than water.

68
Q

Describe how viscosity may change in certain circumstances

A

Viscosity is not an absolute value, depends on:
Haematocrit - 50% increase in haematocrit increases viscosity approx. 100%. The more cells you have the thicker the blood becomes.
Temperature - increase in temp decreases viscosity and vice versa. 1oC changes viscosity by around 2%. This is one of the complications of hyperthermia. The colder you are the thicker you blood and the harder it is to pump the blood around your body.
Flow rate - decreased flow rate increases viscosity and vice versa.

69
Q

Describe the fundamental properties of an adaptive immune response.

A

Distinguishes between different pathogens based on shapes on the surface (these shapes are called antigens )
Slower: Can take few days to develop
Immunological memory: memory cells remember

70
Q

Describe the role of B-Lymphocytes in immunity

A

B cells Involved in humoral immunity

Main function is the production of Abs

71
Q

Define the various classes of naturally occurring amino acids.

A
Aliphatic = hydrocarbon in R group 
Aromatic = Hydrocarbon ring in R group 
Sulphur-Containing = Sulphur in R group 
Acidic = 
Basic = 
Polar = polar R group
72
Q

Describe the functions of proteins.

A

Proteins perform crucial roles in biological processes.
Proteins may be structural (e.g. actin ‘scaffold’ within a cell or keratin in skin) or functional (e.g. catalytic function of enzymes or antibodies in immune defence)

73
Q

Define the terms ‘primary structure’, ‘secondary structure’, ‘tertiary structure’ and
‘quaternary structure’ as applied to proteins.

A

Primary structure = This is the sequence in which amino acid monomers are bonded together to form a polypeptide chain.
Secondary structure = This is the 3D spatial arrangement of amino acids located near each other in the polypeptide chain. Secondary structure relies on hydrogen bonding between the amino hydrogen of one amino acid and the carboxyl oxygen of another amino acid in the same chain.
Tertiary structure = Tertiary structure results when functional groups of ‘R’ chains of amino acids in the polypeptide chain interact with one another. Van der Waals, ionic, hydrogen, disulphide bridges and hydrophobic interactions can all be involved
Quaternary structure = Sometimes several polypeptides interact with one another to form a quaternary structure (e.g. haemoglobin contains four highly-folded polypeptide chains and four iron-containing heme groups, with one group tucked within the interior of each folded polypeptide subunit)

74
Q

Discuss the particular properties that the possession of quaternary structure may
confer on a protein.

A

-

75
Q

Compare the structures and functions of fibrous proteins with those of globular
proteins.

A

Globular proteins are used for: Storage as Enzymes, Hormones Transporters and for Structural.
Fibrous proteins are sued for Muscle fibres Connective tissue

76
Q

Discuss the ways in which enzymes catalyse reactions.

A

Lower activation energy.
1. Entropy reduction
Enzymes “force” the substrate(s) to be correctly orientated by binding them in the formation they need to be in for the reaction to proceed

  1. Desolvation
    Weak bonds between the substrate and enzyme essentially replace most or all of the H-bonds between substrate and aqueous solution
  2. Induced fit
    Conformational changes occur in the protein structure when the substrate binds
77
Q

Describe the ways in which the rate of an enzyme-catalysed reaction may vary with
changes in the concentration of the enzyme and of the substrate.

A

-

78
Q

Define the term ‘Michaelis constant’, describe how it may be experimentally
estimated and describe what a knowledge of the constant may allow to be deduced
about the nature of the catalysed reaction.

A
  • See slides -
79
Q

Describe the molecular nature of competitive and non-competitive inhibition of
enzyme-catalysed reactions.

A
Competitive = Inhibitor binds to the active site. 
Non-competitive = Inhibitor binds to another site changing the shape of the active site.
80
Q

Understand why enzyme activity is measured in a clinical setting

A

diagnostic reasons?

81
Q

Understand what factors can influence enzyme activity in samples

A

-

82
Q

Discuss the use of enzyme assays in clinical diagnosis

A

-

83
Q

Define the major carbohydrates in the diet.

A
Monosaccharides 
Disaccharides 
Polysaccharides 
Glycoproteins 
Proteoglycans
84
Q

Describe, in outline, their digestion and absorption.

A

Enzymes help to break down the carbohydrates in the mouth and Duodenum. And then completely broken down in the small intestine. Glucose, fructose and galactose are then absorbed across the membrane.

85
Q

Describe and contrast the actions and functions of the enzymes hexokinase and glucokinase.

A

Glucokinase has a low affinity for the substrate while Hexokinase has high affinity for the substrate.
This means that in blood of a normal glucose concentration the liver doesn’t “grab” all of the glucose, so other tissues can have it.
However if the blood glucose concentration is high (i.e. after meal) the liver will “grabs” the Glucose.
At a low blood glucose concentration Hexokinase will however be able to grab glucose effectively.
The high Vmax of glucokinase means it can phosphorylate all the Glcose it traps quickly. This means that most of the absorbed glucose in our bodies is trapped in the liver.
The low Vmax of Hexokinase means tissues are “easily satisfied”, so don’t keep “grabbing” Glc

86
Q

Describe the synthesis and degradation of glycogen.

A

Glycogen does not form directly from Glcose monomers.
Glycogenin begins the process by covalently binding Glcose from uracil-diphosphate (UDP)-glucose to form chains of approx. 8 Glc residues
Then glycogen synthase takes over and extends the Glc chains.

87
Q

Compare and contrast the functions of glycogen in skeletal muscle and liver.

A

In the liver If blood Glucose concentration falls the G6P can be converted back into glucose which can be released into the blood.
However in skeletal muscle there is no glucose 6-phosphatase (not produced in skeletal muscle) so therefore glycogen is converted to ATP (energy).

88
Q

Describe the function and process of glycolysis.

A

Glycolysis sits in the middle of most metabolic pathways.
Glycolysis is a catabolic pathway that saves some potential energy from glucose/G-6-P by forming ATP through substrate level phosphorylation
It is essentially the only way that energy can be made from fuel molecules when cells lack O2 (exercising muscle) or mitochondria (RBCs)
Gene sequencing has revealed that it is an ancient process, conserved through organism. It is though to have evolved before atmospheric O2 was plentiful. And it occurs in cytosol with no complex organelles required.
It is therefore important to life and justifiably fills the central role in the metabolic pathways

89
Q

Describe the functions of the lactate dehydrogenase- and pyruvate dehydrogenase - catalysed reactions.

A

-

90
Q

Describe the fate of blood lactate.

A

a

91
Q

Describe the precursors for, functions of and process of gluconeogenesis.

A

a

92
Q

Describe, in brief, the fates of absorbed galactose and fructose

A

a

93
Q

Describe the functions and process of the citric acid cycle.

A

a

94
Q

Identify reactions that involve electron carriers

A

a

95
Q

Identify reactions that release CO2

A

a

96
Q

Describe links to other metabolic pathway

A

a

97
Q

Describe, in outline, the pathway of electron movement from reduced substrates to
oxygen in the mitochondrion.

A

a

98
Q

Describe, in outline, the generation of a proton concentration gradient across the
inner mitochondrial membrane, and how this is used to convert ADP to ATP.

A

a

99
Q

Define the major lipid classes and their role in health and disease

A

a

100
Q

Describe in outline the processes of lipid digestion and absorption.

A

a

101
Q

Describe how lipids are transported in the body and the role of lipoproteins in this
process.

A

a

102
Q

Describe the synthesis of free fatty acids and define the term ‘essential fatty acid’.

A

a

103
Q

Describe the catabolism of fatty acids by beta-oxidation.

A

a

104
Q

Describe the structure and functions of cholesterol.

A

a

105
Q

Describe the structure and functions of eicosanoids and steroid lipids

A

a

106
Q

Describe the function, synthesis and metabolism of ketone bodies.

A

a