Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

My MGD > Semester 1 > Flashcards

Semester 1 Flashcards

1
Q

Hydrophobic

A

Will not interact with water e.g. Lipids (means that they can pass through lipid bilayers)

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

Hydrophilic

A

Polar, interacts with water. Reduces storage ability - cannot pass through lipid bilayers unassisted.

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

Roles that proteins play

A 
Catalysts (enzymes)
Transporters (haemoglobin)
Structural support e.g.Collagen (in skin and bones)
Machines (muscular contraptions- actin)
Immune protection (antibodies)
Ion channels
Receptors e.g. Hormones
Ligands in cell signalling
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Cytoplasm role

A

Metabolism of carbohydrates, amino acids and proteins.

Fatty acid synthesis

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

Lysosomes

A

Membrane bound structure with digestive enzymes - cellular digestion

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

Golgi complex

A

Series of flattened sacs with associated vesicles. It is involved in the export of proteins (modifies them chemically, sorts and packages them) and carries out detoxification reactions

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

Plasma membrane

A

Controls what goes in and out of the cell, cell morphology and transport

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

Mitochondria

A

Long structures with a double membrane. The inner membrane is folded to form cristae. It is involved in ATP production,

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

Endoplasmic reticulum

A

Network of membranous tubules in the cytoplasm. Involved in detoxification reactions, protein synthesis (RER), export of proteins, membrane synthesis and lipid and steroid synthesis

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

Nucleus

A

Round body surrounded by nuclear envelope. Contains nucleolus with RNA and DNA. Used for DNA synthesis and repair, RNA synthesis, RNA processing and ribosome Assembly and transport of ions and small moelcules

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

Ribosomes

A

Small particles in the cytoplasm or attaches to Endoplasmic reticulum made of protein and RNA. For protein synthesis

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

Base

A

Accepts protons

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

Acid

A

Donates protons

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

Conjugated proteins

A

Proteins containing covalently linked chemical components in addition to amino acids

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

Aliphatic

A

Straight chain of carbon atoms only

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

Aromatic

A

Benzene rings

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

Pk

A

Acid dissociation constant - The higher the pKa value the lower the tendency of the acid to dissociate so the stronger the acid

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

Peptide bond characteristics

A

Carbonyl oxygen and Amide hydrogen in trans orientation
No rotation about peptide bond
All atoms involved in the bond are planar

(Planar and rigid)

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

Isoelectric point pI

A

The pH at which there is no overall net charge

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

Basic proteins

A

Have a pI over seven and they include positively charged basic amino acids (lysine, arginine)

21
Q

Acidic proteins

A

PI is less than seven, contains many negatively charged acidic amino acids like glutamate and asparate

22
Q

Primary structure

A

The linear amino acid sequence of the polypeptide chain

Covalent bonds

23
Q

Secondary structure

A

The local special arrangement of the polypeptide backbone

Hydrogen bonds

24
Q

Tertiary structure

A

3D arrangement of the atoms in the polypeptide chain

Covalent bonds
Ionic bonds
Disulphide bridges 
Van der Waals 
Hydrophobic interactions
25
Q

Quaternary structure

A

3D arrangements of the polypeptide sub units

Ionic bonds
Covalent bonds
Van der Waals 
Hydrophobic interactions 
Disulphide bridges
26
Q

Alpha helix

A

3.6 amino acids per turn
0.54nm pitch
Right handed helix
The hydrogen bonds occur between amino acids four residues away from each other
Small hydrophobic residues are strong helix forms (ala and leu)
Pro and gly are helix breakers

27
Q

Beta sheets

A

Fully extended conformation
0.35nm between adjacent amino acids
R groups alternate between opposite sides of the chain

They can be parallel or antiparallel. There are multiple inter strand hydrogen bonds, which are more angular when the sheets are parallel

28
Q

Fibrous proteins

A

Have a structural role, long strands or sheets, single type of repeating secondary structure with little or no tertiary structure e.g. Collagen.
They are insoluble

29
Q

Globular proteins

A

Role in catalysis and regulation. Have a compact shape with several types of secondary structure and a complex tertiary structure. Soluble e.g. Enzymes

30
Q

Motifs

A

Folding patterns containing one or more elements of secondary structures

31
Q

Denaturation

A

Disruption of protein structure

Disulphide bridges - reducing agents
Hydrogen bonds - changes in pH
Ionic interactions - changes in pH
Hydrophobic interactions -detergents

32
Q

Chaperones

A

Assist with protein folding

33
Q

Protein that Fe binds to in myoglobin and haemoglobin

A

Histidine residue

34
Q

Myoglobin

A 
Single polypeptide chain
One haem group
Fixed affinity for oxygen
No cooperative binding
Hyperbolic curve
35
Q

Haemoglobin

A 
Tetramer structure
Two alpha and two beta sub units
Four haem groups
Cooperative binding
Sigmoidal curve
Exists in T and R state - T state is low affinity as binding site is less exposed - conformation changes in the R state
36
Q

3 things that reduce affinity of haemoglobin to oxygen

A

BPG (2,3 bisphosphoglycerate)
H+
CO2

37
Q

Sickle cell anaemia

A

Mutation of glutamate to valine in beta globin.
Polymerisation of haemoglobin occurs as sticky hydrophobic pockets form
They are rigid so may block microvasculature and also lyse (release contents)

38
Q

Thalassaemias

A

Group of genetic disorders where there is an imbalance between the number of alpha and beta globin chains.

Beta is when there are decreased or absent beta chains. The alpha ones cannot form stable tetramers.

The alpha one is where the alpha chains are absent and beta ones are able to form stable tetramers but they have an increased affinity for oxygen.

39
Q

Transition state

A

High energy intermediate that lies between the substrate and product

40
Q

Activation energy

A

Minimum energy that the substrate must have for the reaction to occur.

41
Q

Enzymes

A

Biological catalysts that increase the rate of reaction by finding an alternative pathway with a lower activation energy

42
Q

Features of enzymes

A 
Highly specific
Unchanged after a reaction
Do not affect the reaction equilibirum 
Increase the rate of reactions
Proteins 
May require assisted cofactors
43
Q

Km

A

The substrate concentration that gives half the maximum rate of reaction

44
Q

Vmax

A

The maximum rate of reaction which occurs when all the active sites of the enzymes are saturated with the substrate

45
Q

Enzyme inhibitors

A

Molecules that slow down or prevent an enzyme reaction

Irreversible -covalent bonds
Reversible - non covalent bonds that can freely dissociate

46
Q

Competitive inhibition

A

Bonds to the active site, competition between the inhibitor and the substrate. Km increases but V max stays the same as adding enough substrate overcomes the effect of the inhibitor

47
Q

Non competitive inhibition

A

Binds to a site other than the active site which changes the shape of the active site. Vmax decreases but Km stays the same.

48
Q

Basic positively charged amino acids

A

Lysine

Arginine

49
Q

Amphiphatic

A

Molecules with a polar and non polar region at either end

My MGD (1 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions