Sept 8 Protein Structure Flashcards

(54 cards)

1
Q

what are the bonds linking amino acids together?

A

peptide bonds

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2
Q

what is the basic biological point of DNA and RNA?

A

to allow the synthesis of specific proteins which carry out the chemical and physical functions of cells

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3
Q

what is the size of the smallest proteins?

A

~40 amino acids in length

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4
Q

what is the average size of a protein?

A

~300-400 amino acids

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5
Q

what is the largest known protein and how many amino acids long?

A

titin, muscle protein
~30,000 amino acids

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6
Q

what is the primary structure of proteins?

A

the specific sequence of amino acids

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7
Q

what kinds of shapes are created?

A

definite 3-D structures depending on the sequence of amino acids

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8
Q

what determines the function of a protein?

A

its overall shape (specific folding pattern) and the distribution of amino acids with distinctive chemical properties throughout the overall shape

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9
Q

what are the two major classes of amino acid side chains?

A

hydrophilic
water loving
polar electronic charge distribution
interact well with water

hydrophobic
non polar charge distribution
do not interact well with water

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10
Q

what is the hydrophobic effect?

A

water molecules surrounding hydrophobic molecules dispersed in water adopt a constrained, cage like organisation, which has low entropy (stable)

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11
Q

what happens if hydrophobic molecules coalesce? (come together to form one mass or whole)

A

total number of low entropy constrained water molecules is reduced
net increase in entropy
separate hydrophobic and aqueous phases

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12
Q

what favours the coalescence of hydrophobic molecules?

A

weak non covalent van der waals intermolecular interactions

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13
Q

what is the secondary structure of proteins?

A

local folding and hydrogen bonding
(alpha helix or beta sheets)

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14
Q

what is the tertiary structure of proteins?

A

overall conformation
spatial organization of the multiple secondary structure elements

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15
Q

what is the quaternary structure of proteins?

A

multimeric structure (when multiple proteins come together)

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16
Q

what are supramolecular structures?

A

large scale assembly of proteins

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17
Q

what are the different functions of proteins? (8)

A

structure
movement
molecular transformation
signalling
transport
binding
catalysis
regulation

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18
Q

what dictates the protein structure and function?

A

the amino acid sequence (primary structure)
indirectly determined by DNA

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19
Q

what proportion of a polypeptide do alpha helix and beta sheets occupy? and what is the rest?

A

60%
the rest is made of irregular structures, coils and turns, or is disordered.

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20
Q

where does the bonding occur to create those structures?

A

peptide bond carbonyl O atoms on one amino acid and amino group hydrogens on a different amino acid residue

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21
Q

what is the gross structure of an alpha helix?

A

a straight rod

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22
Q

what is an important covalent bond interaction that is important in an amino acid?

A

side chain of amino acid cysteine contains sulfhydryl group that can form covalent S-S (disulfide) bonds with other cysteine side chains

23
Q

where can those disulfide bonds be found and what do they contribute to?

A

intrachain, contributing to the tertiary structure
interchain, contributing to the quaternary structure

24
Q

what is a “motif” in protein structure?

A

combination of secondary structures forming distinct local 3D structure
do not contain enough bonds to maintain shape if it is cut away from the rest of the protein
rest of protein also contributes to its stability
motifs are not structurally independent entities

25
what are protein domains?
larger than motifs (less than 40 AA long) compactly folded can be made of various motifs characteristic 3D structures within proteins could maintain shape if cut away from rest of protein rest of protein contributes little to the stability structurally independent entities, covalently joined to the rest of the protein
26
what are the four major structural classes of proteins?
fibrous proteins globular proteins integral membrane proteins intrinsically disordered proteins
27
what are intrinsically disordered proteins?
proteins or protein segments that exist as random coils under physiological conditions may adopt a specific secondary/tertiary structure upon binging to a well structured partner protein
28
what are supramolecular complexes and an example?
large molecular machines made up of multiple distinct proteins, each of which may contain multiple subunits example: transcription initiation complex
29
what are structural proteins?
determine the shape of cells and their extracellular environments serve as guides to direct the movement of organelles and molecules usually formed by assembly of multiple proteins subunits into very large and very long structures
30
what are scaffold proteins?
bring other proteins together into ordered arrays to perform specific functions more efficiently than if they were separate
31
what are enzymes?
proteins that catalyse chemical reactions
32
what are membrane transport proteins?
embedded in cellular membranes and permit the flow of ions and molecules across the membranes
33
what are regulatory proteins?
signals, switches and sensors to control activities of cells by altering the functions of other proteins and genes
34
what are signalling proteins?
hormones and cell surface receptors and transmit extracellular signals to cell interior
35
what are motor proteins?
responsible for the movement of other proteins
36
what are amino acids sometimes reffered to as?
residues
37
how many residues per turn in an alpha helix? and why is it that number and not a whole number?
3.6 (a 36 amino acid long helix will have 10 turns) not 4 because Hydrogen bonds are tilted
38
how can the different strands be arranged in a beta sheet?
parallel (all strands point to the same side) or antiparallel (the strands point to different sides
39
what is a functional domain?
a region of a protein that exhibits a particular activity characteristic of that protein
40
what is the domain architecture?
the organisation (order) of domains within a multidomain protein
41
what are topological domains?
regions of proteins that are defined by their distinct spatial relationships to the rest of the protein can comprise one or more structural and functional domains
42
what are proteins that have a common ancestor called?
homologs
43
what are globular proteins?
generally water soluble compactly folded structures often spheroidal mixture of secondary structures (both alpha and beta)
44
what are fibrous proteins?
large, elongated often stiff long chain comprised of many tandem copies of a short AA sequence motif that forms a repeating pattern usually play a structural role or participate in cellular movements
45
what is an intrinsically disordered region (IDR)?
a segment of a protein that is very flexible, with no fixed well ordered conformation if the entire protein has no well ordered conformation, is it called an intrinsically disordered protein (IDP)
46
what is the native state of a protein?
one or a few closely related conformations that proteins are in when they are in their normal functional states
47
what is metabolic coupling?
when proteins assemble together to be more efficient
48
what are biomolecular condensates?
membraneless compartments in cells, often compared to liquid droplets chemically and physically distinct from their surroundings can break apart into smaller droplets or fuse together
49
what affects the capacity of proteins to form condensates?
depends on their structures and the surrounding environment (pH, temperature etc)
50
between what elements are hydrogen bonds created in protein secondary structure?
between carbonyl O (C double bond O) atoms on one amino acid and the amino group H (N--H) on another amino acid
51
which amino acid binds to which amino acid in an alpha helix?
amino acid n bonds with amino acid n+4 (1 to 5, 2 to 6, 3 to 7 etc)
52
explain how the coiled-coil motif is oriented/works?
heptad repeat of amino acids, and amino acids 1 and 4 are hydrophobic hydrophobic amino acids cannot be exposed to water therefore two molecules join together (2 coils)
53
how are side chains arranged in a beta sheet and how does that affect the protein?
side chains protrude above and below the plane of the beta sheet determines the interactions of the beta sheet with other parts of the protein and also its propensity to form
54
what type of stereoisomers are amino acids?
L stereoisomers it's the way it was chosen by nature