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medical science xy1110 > into to amino acids and proteins > Flashcards

into to amino acids and proteins Flashcards

exam 2

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1
Q

what is the central dogma of molecular biology

A

The flow of genetic information from DNA to RNA to proteins can be represented by a scheme called the central dogma of molecular biology

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2
Q

what is the information in DNA used for

A
  • three nucleotides make a codon
  • triplets code for amino acids
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3
Q

what is the exceptions to the universal code

A
  • some organisms have slight modifications eg. mitochondria
  • triplets code for different amino acids
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4
Q

greek name for protein

A

proteios meaning primary

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5
Q

what are the components of proteins

A

C,H,O,N (approx 16%) and sometimes S

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6
Q

what is the molecular weight of an amino acid

A

110 g mol-1

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7
Q

what is protein mass weighed in and how much does a large bio molecular way

A
  • Daltons (Da)
  • large bio moleucules >10,000 Da
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8
Q

what is the average protein length of amino acids

A
  • 200
  • most between 50 - 2000
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9
Q

functions of proteins

A
  • transport
  • fluid balance
  • source of energy and glucose
  • acid- base balance
  • cell membrane structure and function
  • enzymes
  • hormones
  • immune factors - antibodies
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10
Q

structure of amino acid

A

H2N—-CHR—–COOH
left- amine group
right - carboxyl group
central C - chiral carbon
R- residual group ( variable)

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11
Q

what are the two isomers of amino acids and which are only found in proteins

A

L isomer - only found in proteins - amino group on left side
D isomer - amino group on right side

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12
Q

what are the exceptions to the amino acid characteristics

A
  • Glycine - has no enantiomers as it has two hydrogen groups
  • Proline - a amino group is attached directly to side chain so makes an amide
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13
Q

how many essential and non essential amino acids are there and what do they mean

A

Non essential - 11 - humans can synthesis them
essential - 9 - cannot be synthesised

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14
Q

define peptide, polypeptide and proteins

A

peptide - <40-50 amino acids
polypeptide - >50 amino acids
protein - one or more polypeptides

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15
Q

what is a peptide bond

A

link the alpha amino group to the carbonyl group of the next amino acid

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16
Q

what is the primary structure of a protein

A
  • sequence of amino acids in a single polypeptide chain
  • most related to nutritional value
  • makes the core amino acid backbone
  • determines the chemical and physical characteristics
17
Q

where does hydrogen bonding occur in the primary structure

A

backbone due to carboxyl group and hydrogen atoms bonded to amine group

18
Q

cause, signs and treatment of sickle cell anaemia

A

cause - single error in amino acid sequence of haemoglobin

signs -anemia, chest, abdomen and join pain,
swollen hands and feet, frequent infections, stunted growth and vision problems

treatment - drug therapy, blood infusions, supplemental oxygen, bone marrow transplants, gene therapy

19
Q

what is the secondary structure of a protein

A

folding of a protein due to hydrogen boding between elements in the amino acid backbone forming alpha helix or beta folded sheets

20
Q

where do hydrogen bonds form in an alpha helix

A

every 4th amino acid forming a helical structure

21
Q

what are the two type of beta folded sheets and how are they formed

A

antiparallel - amino acid strands run opposite directions

parallel - amino acid strands run the same direction

  • rows of amino acids are liked by hydrogen bonds
22
Q

where do loops form

A

outside of proteins when the protein folds into its tertiary structure

23
Q

what are loops used for and what are their properties

A
  • often binding sites for other molecules
  • rich in hydrophilic residues as they are exposed to water
24
Q

why are weak bonds important in polypeptides

A
  • many weak bonds act in parallel to hold two regions tightly together
  • stability determined by the number of non covalent bonds
25
Q

what is the tertiary structure of a protein

A
  • 3D folding and coiling of the polypeptide forming a globular structure
  • maintained by ionic bonds, disulphide bridges and hydrogen bonds aswell as hydrophobic interactions
  • contains multiple secondary structures
26
Q

what are homomers

A

proteins made of all of the same sub unit

27
Q

what are oligomers

A

proteins made of multiple subunits

28
Q

what are heteromers

A

proteins made of different subunits

29
Q

what is a proteins quaternary structure

A
  • interactive folding of several polypeptide chains forming a single functional protein
  • subunits held together by non covalent forces
30
Q

what are protein domains

A
  • a unit of organization distinct from the four structures
  • usually contain 40 to 35- amino acids
  • different domains are associated with different functions
31
Q

how are protein domains formed

A

a substructure is produced by any part of the polypeptide chain and is folded interdependently into a compact, stable structure

32
Q

what is sequence alignments used for

A
  • identifys homologous protein domains
  • uses short signature sequences
33
Q

what is paralogous

A
  • homologous sequence separated via a gene duplication event
  • a gene in an organism is duplicated to occupy two different positions in the same genome these two copies are paralogous
34
Q

what is orthologous

A
  • homologous sequence separated via a speciation event
  • species diverges into two separate species the copies of single gene in both species are said to be orthologous
35
Q

what is post translational modification and what does it involve

A
  • allows the newly made polypeptide chain to become fully functional
  • involves 3D shaping and/or adding methylation and phosphorylation
36
Q

how are proteins further modified

A
  • attachment of carbohydrate, lipid or RNA groups
  • attachment of small
    inorganic and organic molecules eg. metal ions, vitamins, methyl groups and phosphorylation
37
Q

what are cofactors

A

usually metal ions or small organic molecules necessary for protein activity

medical science xy1110 (33 decks)

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