special topic 2 - protein structure Flashcards

1
Q

what atoms are amino acids all made of

A

C, O, N, H and occasionally S

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2
Q

what is the alpha carbon

A

the central carbon of an amino acid (stereogenic centre)

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3
Q

how is the polymerisation of amino acids reversed

A

hydrolysis reaction to return to amino acid monomers

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4
Q

describe the joining of amino acids

A

large ribosomal unit catalyses dehydration condensation reaction in which carboxyl and amino groups join to form peptide bond.

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5
Q

4 possible characteristics of amino acids

A

hydrophobic, hydrophilic, acidic and negatively charged, basic and positively charged

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6
Q

differentiate between an amino acid and a residue

A

amino acids are usually referred to as residues once in a polypeptide chain

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7
Q

what is the secondary structure

A

local folding of the polypeptide chain - the beginning of hydrogen bonding and folding. alpha helices and beta sheets are formed.

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8
Q

what does the artemis protein do

A

involved in antibody production. without it we would need to live in a sterilised environment.

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9
Q

what is the hydrophobic effect, and its role in proteins

A

the interaction of non-polar or hydrophobic side chains with an aqueous environment, and subsequent burial into the proteins internal environment . important for protein folding, means most hydrophobic residues are found facing inward and hydrophilic residues are found on outside.

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10
Q

what are alpha helices and beta sheets

A

helices are helical structures of spiralling backbones with side chains pointing outwards, with hydrogen bonds maintaining the twisting structure.
beta sheets backbones extend our then double back on themselves, hydrogen bonds extend straight across between backbones.

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11
Q

what is the tertiary structure

A

full folding of polypeptide to make a large structure, this is many proteins final form

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12
Q

what is quaternary folding

A

multiple tertiary polypeptide subunits joining to form a larger protein structure

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13
Q

what is a tetramer and an example of one?

A

4 protein subunits forming a quaternary structure. hemoglobin is a tetramer.

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14
Q

structure of malic enzyme

A

2 dimers joined together

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15
Q

structure, function, and examples of a globular protein

A

globular proteins are highly folded and look like ‘globs’, usually have metabolic function. examples are artemis and alpha amylase.

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16
Q

structure, function, and examples of a fibrous protein

A

tend to be long and spindly, usually involved in structural elements. e.g actin and collagen.

17
Q

what is alpha amylase

A

an enzyme secreted in saliva to break down food

18
Q

four types of bonds holding together proteins

A

hydrogen bonding, electrostatic interactions, disulphide bonds, hydrophobic interactions.

19
Q

how many amino acids can participate in electrostatic interactions, give example of 2

A

5, e.g glutamic acid and lysine.

20
Q

what does code E116 (or similar) refer to.

A

letter corresponds to protein where possible, but is often not the first letter. number indicates number of residues downstream from the N terminus the amino acid is.

21
Q

what is the second strongest type of bond in a protein, explain its structure and location

A

disulfide bond. two sulfide bonds form a disulfide ‘bridge’ between two cysteine amino acids.

22
Q

what are hydrophobic interactions

A

clustering of hydrophobic side chains together away from water

23
Q

explain how an egg becomes insoluble in heat

A

albumin proteins unravel in heat, then the unravelled proteins form new permanent disulfide bonds. proteins can’t return to original folding, become protein aggregate with hydrophobic amino acids on the outside.

24
Q

proteins are _______ stable, as they are both ______ and can be ________

A

marginally stable, are maintained but can be denatured

25
Q

what denatures proteins

A

pH, temperature, salt concentration,

26
Q

what is a protein aggregate

A

large misfolded or damaged protein structures, which often are insoluble and have lost their original function.

27
Q

experimental methods of determining protein structure

A

crystallography, cryo electron microscopy, NMR

28
Q

how does crystallography work

A

protein crystals are made, and their diffraction patterns are used to map electron density to determine atomic structure

29
Q

what does malic enzyme do

A

catalyses conversion of malate to pyruvate, in presence of NAD+/NADP+

30
Q

what is warburg effect/warburg glycolysis

A

the preferential conversion of pyruvate to lactate rather than entering the mitochondria for CAC. it is a crucial part of cancer cells ability to upregulate their own growth.

31
Q

what role does malic enzyme play in cancer

A

in warburg conditions in cancer cells, glutamine amino acid is used to make malate, which magic enzyme converts to pyruvate for acetyl CoA to fuel CAC

32
Q

what is NPD-389, what is its medicinal function

A

an inhibitor for the malic enzyme, which malate competes unsuccessfully for. used in anti-cancer, as it disables cancer cells from making pyruvate for the CAC via malic enzyme.

33
Q

ben krinkel’s new drug potency proportionate to NPD-389

A

4 times as potent