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FunMed Genetics > Protein > Flashcards

Protein Flashcards

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Biology 101 flashcards
1
Q

what are the roles of the proteins

A
  • Structural – cytoskeleton
  • Catalysts – enzymes (anabolic and catabolic)
  • Carrier/storage - haemoglobin
  • Protective - antibodies
  • Signalling – receptors, intracellular signalling
  • Channels – transport through membranes
  • Transporters – transport through membranes and barriers
  • Cell adhesion – extracellular matrix
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2
Q

structure and function are….

A

linked, they impact each other

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3
Q

what are the level of structures of proteins

A
  • Primary – sequence of amino acids from the N-terminus to the C-terminus
  • Secondary – 2d fold
  • Tertiary – 3d fold
  • Quaternary – interaction of multiple subunits
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4
Q

what is the function of the protein determined by

A
  • The function of the protein is determined by its chemistry on the outside and the shape, this is determined by the amino acid sequence
  • Different amino acids have different R groups which have different properties chemically and structurally
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5
Q

what is the amino acid made out of

A
  • Made out of an amino group NH2
  • R group – gives the chemical and physical properties - varies between 20 different amino acids
  • H on the carbon
  • Carboxyl group COOH
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6
Q

what are the different chemical properties of R groups

A
  • Hydrophobic/hydrophilic
  • Polar (have an electrical charge) and non polar(don’t have an electrical charge)
  • they have overlapping properties
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7
Q

how do we join amino acids together

A

peptide bonds

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8
Q

describe the peptide bond

A
  • Impacts structural implications – can be planar and H bonding
  • Looses water forms CONH bond, looses H from NH2 and looses OH from COOH
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9
Q

what does planar mean

A

rigid, cant bend around the peptide bond and therefore this restricts the 3D shapes that are available

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10
Q

whats the minimal number of amino acids in a protein

A

50

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11
Q

what is the typical number of amino acids in a protein

A
  • 50-2500 amino acids make a typical protein but it can be as many as 5000
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12
Q

describe what determines the secondary structure

A
  • This is determined by the interactions between the peptide bonds via hydrogen bonding
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13
Q

what are the two types of secondary structure

A

alpha helix and beta pleat

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14
Q

describe the alpha helix

A
  • 3.6 residues per 360deg turn, a 0.54nm pitch - this means residues are travelling forward
  • Stabilised by hydrogen bonding between the peptide bonds carboxyl group and amino group further down
  • R groups point outwards due to the peptide chain
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15
Q

why is proline not found in an alpha helix

A
  • Proline has problems being in an alpha helix, because most R groups go out from the central carbon and doesn’t reconnect, this means that proline cant twist and bend in the same way that other amino acids can, therefore proline is not in an alpha helix but rather at the beginning and end where it breaks the alpha helix
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16
Q

describe the beta sheet

A
  • Hydrogen bond run across to stabilise it
  • Beta sheets can be stacked to form a 3D tertiary structure
  • Strands can be parallel or anti-parallel
  • forms a flat surface sheet with strands of protein alongside
  • Stabilised by hydrogen bonds between amide links
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17
Q

what are the two subclasses of beta sheets

A

parallel and antiparallel

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18
Q

describe parallel

A

parallel sheet the strands go in the same direction from N-terminus and C- terminus

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19
Q

describe antiparallel

A

Antiparallel is where the strands go one way and then another

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20
Q

describe disorder

A
  • third type of secondary structure
  • This is a concept of key forming in the lock
  • Disordered regions of proteins often involve protein interaction and are often rich in polar residues so they are hydrophilic
  • Cant form on its own
  • Often on the surface of the protein
  • Amino acids tend to be hydrophilic
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21
Q

describe the tertiary structure

A
  • Tertiary structure is the 3D fold of the protein which brings the secondary structure into 3D space
  • Held together by interactions between the R groups
  • Huge variety of different structures possible
  • R group is central
  • Can be globular or fibrous
  • Globular = water solution for example haemoglobin
  • Fibrous = insoluble such as collagen and keratin
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22
Q

describe the quaternary structure

A
  • A fold of 3D folded subunits
  • Not all proteins have this some stop at tertiary
  • Can be homo or hetero
  • Homo – subunits are the same
  • Hetero – mixture of subunits
  • E.g. haemoglobin and collagen
  • Large scale quaternary protein complexes are in a viral capsid e.g. SV40 - can have loads of subunits
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23
Q

what does homo mean

A

subunits are the same

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24
Q

what does hetero mean

A

mixture of subunits

25
Q

describe collagen

A
  • Fibrous
  • 3 polypeptides
  • Hydrogen bonding
  • Triple helix with a large number of prolines in a pro-pro-gly motif
  • Collagen has to be strong as it forms part of the structural part of the protein
  • Staggering of prolines between three chains helps hydrogen bonding between chains, forms a rigid structure
  • Further post translational modification or amino acid side chains enable covalent strand cross links which include disulphide between cysteines and lysine cross linking
  • vitamin C is important as it is a cofactor of propyl hydroxyls
  • modified proline known as hydroxyproline
  • 35% glycine amino acid as every 3rd residue is
26
Q

what are the two types of proteins

A

globular and fibrous

27
Q

describe globular proteins

A

majority of proteins are globular

- Overall globular shape with a mixture of secondary structures

28
Q

describe fibrous proteins

A
  • Extensive packing of secondary structure
  • Dominated by one type of secondary structure
  • Forms structural proteins such as collagen and keratin
29
Q

what are domains

A

these are discrete regions of 3D structures

30
Q

how is folding driven

A
  • the hydrophobic effect

- hydrogen and polar bonding

31
Q

what does spontaneous folding do

A

minimises the energy

32
Q

not all proteins can….

A

spontaneously fold for example the entire protein may need to be present

33
Q

describe the hydrophobic effect

A
  • wants to reduces the surface of a fat that interacts with water, this drives the folding to happen
  • It creates a Hydrophobic centre
34
Q

what is the exception to the hydrophobic effect

A

membrane protein

- inside the membrane you want hydrophobic effect works in reverse and it folds in the opposite way

35
Q

what is nomenclature

A

the naming of proteins and 3D structures

36
Q

what would make the protein unfold

A
  • temperature
  • pH
  • detergent - destroys hydrophobic effect
  • electric field
  • Putting energy into the system, this changes the bonding and causes the protein to unfold
37
Q

whats another word for heat shock proteins

A

chaperones

38
Q

what do chaperone proteins do

A
  • help proteins refold when they are under stress

- some proteins need them to help them fold normaly

39
Q

what causes chaperones to increase

A
  • Helper proteins – molecular chaperones which helpd fold many proteins
  • Levels of chaperones increase when the cell is subjected to stress such as heat shock, but there present most of the time anyway
40
Q

how do chaperone proteins help refold

A

HSP70 - heat shock protein 70

  • Some act to protect the folding protein from the cytoplasm – ie a unique environment such as GroEL
  • Chaperones often use ATP to provide energy to the folding process
41
Q

what are the causes of protein folding and diseases

A
  • inherited mutation

- environmental stress

42
Q

what is the mechanism of protein folding and disease

A
  • Loss of function
  • Toxic gain of function
  • Dominant negative
43
Q

what are the diseases associated with a malfunction in protein folding

A 
Neurodegeneration 
-	Alzheimers 
-	Parkinsons
Metabolic disorders 
-	Monogenic obesity 
Cancer 
-	P53
44
Q

what is post translational modification

A
  • process of adding more things to protect it
45
Q

what are the types of post translation modification

A 
phosphorylation 
disulphide bridge
cleavage 
membrane anchors
ublinquitination 
deamindation
46
Q

describe phosphorylation

A
  • Process of adding phosphate group to the protein this is catalysed by phosphorylation kinase causes ATP to become ADP
  • Dephosphorylation phophastase catalyses the removal of a phosphate from a protein
  • Allows you to have an on and off swtich, in one state protein is on and in another state protein is off
47
Q

describe disulphides

A
  • Covalent link between cystine residues, cysteine contains sulfur
  • Go from two chains that did not have a covalent link together to chains that do have a covalent link
  • Stabilises a 3D structure
  • Requires specific environment to form, often found extracellularly
48
Q

describes cleavage

A
  • Insulin as a long polypeptide
  • Cleave it twice to form two separate chains
  • Have insulin forms disulphide bridges, cut out a chain and then leaves 2 chains together that give insulin its shape and allows it to carry out its function
49
Q

describe membrane anchors

A
  • Add lipids to proteins modifies them
50
Q

describe ubiquitnation

A
  • Small protein added to another protein
  • added ubiquitin to lysine.
  • Acts in signalling and in degradation (disposes of the cells)
51
Q

describe deamination

A
  • Unavoidable chemical reaction in physiological conditions – can be reduced by removing reactive species from the cytosol
  • Results in structural changes and therefore protein damage therefore we want to degrade it – do this in ubiquitination
52
Q

what are the types of post translational modification descriptions

A 
Addition of other functional groups 
-	Acetate, phosphate and lipids,
Addition of other proteins/peptides
-	Ubliquitination, SUMOylation, Neddylation 
Changing the chemical nature of amino acids 
-	Deamination, eliminylation 
Structural changes 
-	Disulphide, cleavage
53
Q

What is the bond between two amino acids caused by

A

A condensation reaction in which water is lost

54
Q

what is the carbon in the middle of the amino acid called

A

known as a chiral carbon as it is attached to four different groups (apart from glycine)

  • have two different structures which are mirror images of each other but are non superimposable
  • two forms are D and L
  • we use L in cells
55
Q

what are the bonds holding the tertiary structure together

A
  • hydrogen bonding
  • ionic bonding
  • disulphide bridges
  • hydrophobic and hydrophilic interactions
56
Q

globular is ..

A

soluble because they have hydrophilic R groups surrounding the outer aspect that can interact with water

57
Q

fibrous is ..

A

insoluble

- made up of many polypeptide chains such as keratin

58
Q

name some examples of chaperone proteins

A

Hsp70

Hip90

59
Q

what is the primary structure

A
  • Chain of amino acids connected by peptide bonds
  • Protein is greater than 50 amino acids joined together, there are 20 different amino acids
  • Ribosome come out of the N-terminus
  • Leaves from C-terminus

FunMed Genetics (12 decks)

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