BioMed Flashcards
Structure of a standard eukaryotic cell
> diverse in shape, structure and function
> Plasma membrane
> Nucleus
> Mitochondria
> Internal membrane bound organelles
Describe structure and function of cytoskeleton
> Helps cells maintain their shape and internal structures
> Provides mechanical support that lets cells carry out division and movement
Difference between prokaryotes and eukaryotes
> Prokaryotes: no nucleus, contains plasmids, usually unicellular, about 1-10 micrometers
> Eukaryotes: contains nucleus, usually multicellular, 10-100 micrometers
Primary structure of protein
Sequence of amino acids
Secondary structure of protein
Folding; alpha helix and beta pleated sheet
Tertiary structure of protein
3D shape; Defined by the hydrophilic and hydrophobic interactions between R groups of amino acid chains.
di-sulphide bridges
quaternary structure of a protein
A number of polypeptide chains linked together, and sometimes associated with non-protein groups to form a protein.
What is the action of oxidoreductases? Examples?
Reduction and oxidation reactions
Examples:
Dehydrogenase
Oxidase
What is the action of Transferases? Examples?
Transfer of amino, carboxyl, acyl, carbonyl, methyl, phosphate
Examples:
Transaminase
aldolase
What is the action of hydrolyses? Examples?
Change of bonds coupled with inserting water
Examples:
Esterase
Peptidase
What is the action of lyases? Examples?
Cleavage of C-C, C-S, C-N but not peptide bonds
Examples:
Decarboxylase
Aldolase
What is the action of isomerases? Examples?
Rearrangement of bonds
Examples:
Epimerase
Mutase
What is the action of ligases? Examples?
Formation of bonds between carbon and oxygen, sulphur, and nitrogen
Examples:
Synthetase
Carboxylase
What is Km? What does low km mean? high?
> the michealis constant
> Enzyme binds to the substrate tightly and works fast even at a low substrate concentration
> Enzyme binds to substrate weakly and requires a high concentration of substrate to work fast
What is Vmax?
Maximum possible rate of reaction
What are allosteric regulators
Bind to a regulatory site other than the active site and changes the enzyme activity by altering the proteins tertiary or quaternary structure
What are the 6 ways you can regulate enzyme activity
> feedback loops (short term)
> Feed forward activation (short term)
> allosteric regulation (short term)
> phosphorylation-dephosphorylation sequence (short term)..aka post-translational modification
> proteolysis (long term)
> Changes in gene expression (long term)
What enzyme does phosphorylation require? dephosphorylation?
> Kinase
> Phosphotases
What do irreversible inhibitors do?
Form covalent bonds
What happens to km and Vmax in competitive inhibitors
Km= increases
Vmax=unchanged
> More substrate required to saturate enzyme
What happens to km and Vmax in non-competitive inhibitors
km=unchanged
Vmax=decreases
What is an isoenzyme
Different enzymes the catalyze the same reaction but are subject to different regulatory controls (ex: DAHP synthase for aromatic amino acids)
mnemonic to remember classes of enzymes?
Over The Hills Live Intelligent Ladies
Oxidoreductases, Transferases, Hydrolyses, Lyases, Isomerases, Ligases
3 main uses of lipids
> storage of energy
> forming membranes
> signalling between and within cells
What are the two essential fatty acids?
linoleic acid and linolenic acid
> must be taken in from the diet
What does the delta sign mean when naming fatty acids? Omega sign? What does the first number mean? The second?
> delta=where double bonds are in relation to the carboxylic end
> Omega= where the double bonds are in relation to the omega end
> 1st number=number of carbons
> 2nd number=number of double bonds
What is the other name for a triglyceride? describe it
> Triacylglycerol
> 3 fatty acids join onto a glycerol molecule in the formation of an ester bond
> Main storage form of lipids found in adipose tissue surrounding visceral organs and subcutaneous fat
What are the two types of phospholipids? Give an example of each
> Glycerophospholipids
Example:Phosphatidylserine
Sphingolipids
Example:Sphingomyelin
What is cholesterol based on and what does it do?
> Based on steroid structure
>Decreases membrane fluidity as it packs between other lipids
Name four lipid derivatives
> Vitamin D
Steroid hormones
Bile salts
Eiosanoids
Describe vitamin D
> Synthesised from 7-dehydricholesterol by sunlight
>Required for calcium absorption and bone formation
Describe steroid hormones and give three examples
> derived from cholesterol
>cortisol, oestrogen, progesterone
Describe bile salts
> synthesised from cholesterol in the liver
>secreted from the duodenum to aid absorption of dietary fats
Describe eiosanoids and give two examples
> derived from arachidonic acid
Involved in inflammation response and vascular contraction
prostaglandins and thromboxanes
3 main uses of a carbohydrate
> energy storage
structure
recognition and adhesion
What do monosaccharides consist of
aldehyde or ketones and at least two alcohol groups
What is the structure of an aldehyde?Ketone?
> double bonded oxygen and a hydrogen and an r group (on end)
>Double bonded oxygen with two r groups (in the middle)
What are the 3 monosaccharides?
glucose, fructose & ribose
What is sucrose broken down into? by what enzyme?Lactose?Maltose?
> glucose & fructose by sucrase
Glucose & galactose by lactase
glucose & glucose by maltase
What are glycosaminoglycans? what is their role
> large negatively charged heteropolysaccharides
>roles in the extracellular matrix, acting as lubricants and shock absorbers
What are the four types of phospholipid movements in the membrane?
> lateral diffusion
flexion(movement/bending of tail)
rotation(turning around of tail)
flip-flop(rarely occurs-only with help of flippase enzyme, its when they swap from top layer to bottom layer/vice versa)
Give some examples of small non-polar molecules and how they cross the membrane
> Cross by simple diffusion
>O2,CO2,N2,steroid hormones
Give some examples of small uncharged polar molecules and how they cross the membrane
> Can diffuse but not as easily as small non-polar molecules
>H2O, ethanol, glycerol
Can ions diffuse across the membrane?
no
What do transporters allow
Active or passive diffusion
What are the two types of active transport and what are they driven by
Primary active transport driven by ATP
Secondary active transport driven by co-transport of Na+
What do channels allow for? What type of gated are they
facilitated diffusion
ligand-gated or voltage-gated
Where are ligand-gated ion channels found? what else are they called
> Found at neuromuscular junctions
>Ionotropic receptors or ion-channeled coupled receptors
What do G-protein coupled receptors include?
Receptors for: adrenaline glucagon odour molecules acetylcholine rhodopsin (photoreceptor in retina)
Explain what happens in a g-protein coupled receptor
> Ligand binding site causes activation of associated g protein
activated G protein stimulates enzymes that produce second messages (cAMP)
Causes signal amplification
What is anabolic? catabolic?
> where the body builds and repairs muscle tissue
>where the body breaks down the tissue to replenish depleted energy levels
When does a reaction occur spontaneously?
when Gibbs free energy is negative
What is Gibbs free energy measured in?
in kJ/mol
What food molecules are oxidised to release energy?
carbon-based food molecules
What are activated carriers
biomolecules that store energy in the form of transferrable chemical groups
What is NADP+ usually used in
Anabolic pathways
What usually happens to FAD
usually covalently linked to enzymes and acts as a coenzyme
What is the net result of glycolysis & what does it require
2 pyruvate, 2 ATP, 2NADH
requires 2ATP
What is the Krebs cycle also known as & where does it occur
TCA or citric acid cycle
Occurs in the mitochondrial matrix
Net result of Krebs cycle
3NADH, 1FADH2, & 1GTP
Name some short term ways to control the metabolism
Binding of allosteric inhibitors to alter enzyme activity
Covalent modification such as phosphorylation
Name some long term ways to control the metabolism
Changes in gene expression to alter total amount of enzymes
Changes in proteolysis to alter total amount of enzymes
Percentage of ECF and ICF in the body
20% ECF
40%ICF
Conc. of sodium ions in mmol/L in the ECF & ICF? potassium? calcium?
Sodium: ECF:140 ICF:10
Potassium: ECF:4 ICF:120
Calcium: ECF:1.25 ICF:0.0001
What are four important internal properties?
> temperature
pH
Glucose concentration
Oxygen levels
What is interstitial fluid? Plasma?
> thin layer of fluid which surrounds the bodies cells
>Colourless fluid part of blood, lymph in which fat globules are suspended
Define diffusion and bulk flow
> Net movement down a concentration gradient due to random motion of individual molecules
Movement of water and solutes together due to a pressure gradient
What law describes what happens when gases come into contact with fluids such as blood? Describe it
Henrys law
>Concentration of a gas in a liquid is directly proportional to the solubility and partial pressure of that gas
What are the two equations for pH
pH=-log10[H+]
pH=pKa+log10[A-]
Whats the equation for [H+]
[H+]=10^-pH
What is the equation for pKa
pKa=-logKa
What are the differences between acids and bases
Acids: Low pH high conc of H+ release protons Bases: High pH Low conc of H+ Accept protons
Difference between strong and weak acids
Strong acids almost completely dissociate whereas weak acids only partially dissociate
Strong acids have a low pKa, weak acids have a high pKa
What is pKa
The pH at which the acid is half dissociated
What does it mean when the pH=pKa
Then [A-]=[HA]
buffer resists any change (acid or base)
What does it mean when pH < pKa
Then [HA]>[A-]
buffer resists addition of base
what does it mean when pH>pKa
Then [HA] < [A-]