proteins Flashcards

1
Q

what are amino acids

A

protein building blocks made of amino and carboxylic acids groups, that form polymer chains

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2
Q

what is the name of the smallest and simplest amino acid

A

glycine

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3
Q

what is the central carbon in an amino acid bound to

A

1 amino group, 1 carboxylic acid group, 1 hydrogen and 1 R group

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4
Q

what kind of bond links amino acids

A

peptide bonds

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5
Q

what are amino acids separated by (to be put into groups)

A

the structure of their side chains e.g. hydrophobic, hydrophilic and charged

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6
Q

what are nucleotides and what are they made up of

A

they are the building blocks for DNA and RNA - made up of a sugar, a phosphate group and a base

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7
Q

what is the difference between a DNA nucleotide and an RNA nucleotide

A

DNA = deoxyribose sugar
RNA = ribose sugar

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8
Q

what do we call coding and no-coding regions of DNA

A

coding = exons
non-coding = introns

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9
Q

why do all cells not look the same

A

due to specialisation and differentiation

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10
Q

name 4 structural proteins

A

keratin, collagen, actin and myosin

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11
Q

name 3 transport proteins

A

haemoglobin, transferrin and ceruloplasmin

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12
Q

name 3 hormonal proteins

A

insulin, thyroid stimulating hormone, and adrenocorticotrophic hormone

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13
Q

what kind of proteins are regulatory

A

enzymes

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14
Q

what unit do we use to measure proteins

A

Daltons (Da)

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15
Q

what is the key difference between a protein and a polypeptide

A

their size; polypeptides are <5kDa

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16
Q

how many common amino acids are there

17
Q

name the 5 prosthetic groups conjugated proteins may contain

A

metalloproteins = metal group
glycoproteins = sugar group
phosphoproteins = phosphate group
lipoproteins = lipid group
nucleoproteins = associated with nucleic acid

18
Q

name the 4 sections of protein structure and give a brief explanation of them

A
  • Primary; an amino acid chain
  • Secondary; alpha-helix and beta-pleated sheets - formed via hydrogen bonds (in beta-pleated sheets its between the C=O and N-H)
  • Tertiary; 3D conformation - further coiling or bending due to hydrogen bonds, as well as ionic bonds and disulphide bridges
  • Quaternary; multi-protein assemblies
19
Q

what are ampholytes

A

substances that can either donate or accept an electron

20
Q

what are enantiomers

A

the 2 ways of forming an amino acid as there is 2 different ways to arrange in space - mirror copies

21
Q

what is a chiral carbon

A

a carbon with 4 different groups attached

22
Q

all naturally occurring amino acids found in living individuals have which configuration: D (dextro) or L (levo)

23
Q

what do we utilise the D/L configuration in amino acids to determine in forensic science

A

can be applied in precise age determination of human remains using teeth - a younger person will have less Dextro configurated amino acids as they have had less time to variate

24
Q

name the 3 special amino acids and why they are special

A

cysteine - contains sulphur (forms disulphide bridges)
glycine - only has hydrogen bonded to it (not chiral)
proline - is cyclic

25
what forms ionic interactions in proteins
the charge difference between the carboxylic acid group and the NH group
26
why do proteins fold
in order to expose the hydrophilic regions and bury the hydrophobic regions
27
what are the 4 subunits in haemoglobin
2 alpha chains and 2 beta chains
28
name 3 ways of determining protein structure through the use of large equipment
X-ray beam line X-ray crystallography nuclear magnetic resonance
29
name the two ways forensic scientists find evidence containing proteins
luminol and bluestar
30
what is the luminol test based on and what is one drawback
The test is based on the ability of the luminol molecule to be oxidised by the reaction of sodium perborate with an oxidising agent such as haemoglobin False positives with some household chemicals
31
why is bluestar better than luminol
more sensitive, easier to mix in the field, more stable and does not destroy DNA