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Fundamentals of Life Science > Amino Acids & Proteins > Flashcards

Amino Acids & Proteins Flashcards

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Biology 101 flashcards
1
Q

Are fibrous proteins water soluble?

A

no

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2
Q

Are globular proteins water soluble?

A

yes

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3
Q

What is the role of fibrous proteins?

A

structural

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4
Q

What is the role of globular proteins?

A

dynamic (e.g enzymes and receptors)

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5
Q

What is an example of a part globular, part structural protein?

A

myosin

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6
Q

What percentage of dry cell weight do proteins represent?

A

50%

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7
Q

What is the role of proteins?

A

to perform the functions essential for life

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8
Q

know the structure of an amino acid

A

Carboxyl group
Amino group
R group
H atom

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9
Q

What causes the folding of proteins?

A

The hydrophobic effect (driven by the need of internalise hydrophobic polypeptide chains) (polar chains on outside, non-polar on inside)

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10
Q

What is pKA?

A

PH value at which a weakly ionising group is 50% associated

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11
Q

What is the role of di-sulfide bridges?

A

Hold polypeptide chains in shape

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12
Q

What is the most hydrophobic amino acid?

A

phenylalanine

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13
Q

What are the aromatic amino acids?

A

phenylalanine tyrosine tryptophan

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14
Q

What is the primary structure?

A

linear sequence of amino acids

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15
Q

What is the secondary structure?

A

regions of regularly repeating conformations of the peptide stabilised by hydrogen bonding between the peptide groups e.g alpha helices and beta sheets

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16
Q

What is tertiary structure?

A

the 3D shape of the folded chain. Arrangement of all amino acids including R groups and any prosthetic groups (in a single polypeptide chain)

17
Q

What is the quaternary structure?

A

the arrangement of two or more polypeptide subunits in an oligomeric protein (multi chain only)

18
Q

How is a peptide bond formed

A

removal of O from one peptide and 2 H from the other O=C-N-H

19
Q

which amino acids have ionising side chains?

A

Asp, Glu, His, Arg, Ly, Tyr and Cys

20
Q

How do we know that ionising side chains have an affect on protein structure and function?

A

Use electrophoresis to separate proteins and amino acids at different PHs, because they carry different charges at different PHs

21
Q

How do you write an amino acid

A

C terminus first. N terminus on right

22
Q

Describe the structure of a right handed alpha helix

A

Each C=O is hydrogen bonded with the amide hydrogen of the residue 4 places ahead

23
Q

What’s an example of an alpha helix

A

Alpha keratin

24
Q

What’s an example of a beta pleated sheet?

A

virus coat proteins

25
Q

Differences between alpha helix and beta sheet?

A

Alpha helix more compact

-look at structures

26
Q

Describe the tertiary structure of Mb

A
  • contains a heme group
  • globular
  • folded to be very compact (with hydrophobic on inside)
  • 75% of amino acids folded into a right handed alpha helix
27
Q

Why is Hb an allosteric protein?

A

It has multiple ligand binding sites

28
Q

What is the structure of Hb made up of?

A

Two molecules of alpha globin
Two molecules of beta globin
Tetramer organised into a pair of dimers
Largely alpha helical

29
Q

What is collagen?

A

A major protein in vertebrae connective tissue (25-35% of total proteins in mammals)

30
Q

What is collagen made up of?

A
  • Units of the triple stranded tropocollagen molecule. The triple helix is held together by H bonds between chains.
  • multiple repeats of -Gly-X-Y (where X is often proline and Y is often hydroxyproline)
  • Three left handed helical chains coiled around each other in a right handed supercoil
31
Q

What is an enzyme?

A

Usually a protein (can sometimes be RNA) that accelerates biological reactions

32
Q

Why are enzymes important for life?

A
  • Accelerates metabolic reactions
  • enables regulation of metabolic reactions
  • integration of metabolism
33
Q

What are the biomedical applications of enzymes?

A
  1. Diagnostic reagents (e.g enzymes being released into blood after tissue damage)
  2. Lab reagents
  3. Drug metabolism
  4. Drugs work by inhibiting enzymes
34
Q

What are isozymes?

A

Tissue-specific physically distant form of an enzyme

Fundamentals of Life Science (28 decks)

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