into to amino acids and proteins Flashcards

exam 2

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
what is the tertiary structure of a protein
- 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
what are homomers
proteins made of all of the same sub unit
27
what are oligomers
proteins made of multiple subunits
28
what are heteromers
proteins made of different subunits
29
what is a proteins quaternary structure
- interactive folding of several polypeptide chains forming a single functional protein - subunits held together by non covalent forces
30
what are protein domains
- a unit of organization distinct from the four structures - usually contain 40 to 35- amino acids - different domains are associated with different functions
31
how are protein domains formed
a substructure is produced by any part of the polypeptide chain and is folded interdependently into a compact, stable structure
32
what is sequence alignments used for
- identifys homologous protein domains - uses short signature sequences
33
what is paralogous
- 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
what is orthologous
- 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
what is post translational modification and what does it involve
- allows the newly made polypeptide chain to become fully functional - involves 3D shaping and/or adding methylation and phosphorylation
36
how are proteins further modified
- attachment of carbohydrate, lipid or RNA groups - attachment of small inorganic and organic molecules eg. metal ions, vitamins, methyl groups and phosphorylation
37
what are cofactors
usually metal ions or small organic molecules necessary for protein activity