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NUT1004 > Protein Structure > Flashcards

Protein Structure Flashcards

1
Q

Which type of protein tends to feature a single type of secondary structure

A

Fibrous proteins

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2
Q

Which type of protein tends to feature more than one type of secondary structure

A

Globular proteins

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3
Q

What are the two prominent secondary structural arrangements

A

a helix and beta conformation

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4
Q

What is the primary sequence

A

Sequence of amino acid residues involving all covalent bonds (peptide and disulphide) in a polypeptide chain

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5
Q

What is the secondary structure

A

Stable arrangements of AA residues leading to recurring structural patterns

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6
Q

What is the tertiary structure

A

All aspects of 3 dimensional folding of a polypeptide

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7
Q

What is the quaternary structure

A

Spatial arrangement when a protein has more than one polypeptide subunits

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8
Q

What are AA residues

A

AAs joined by a peptide bond

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9
Q

What does the primary structure determine

A

3D structure and functions of the polypeptide/protein

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10
Q

Where do disulphide linkages occur in proteins

A

Cross links formed by adjacent cysteine residues involving the same PP chain or to link two PP chains

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11
Q

What two chains does a PP consist of

A

Main chain (backbone) of repetitive peptide bonds and alpha carbons and variable side chains

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12
Q

How is the PP backbone/main chain both rigid and flexible in the primary structure

A

Rigid as peptide bond is planar owing to partial double bond character as they partially share electron pairs (C=O and C=N) but flexible as limited rotation possible in either side of the alpha carbon

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13
Q

What bond forms the secondary structure and where are they

A

Hydrogen bonds between the peptide NH and CO groups

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14
Q

What is the importance of hydrogen bonding in the secondary structure

A

Causes polarity in the C=O, N-H and O-H groups are attraction between positive and negative charges

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15
Q

How many A residues are in each Tuen of the alpha helix

A

3.6 AA residues

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16
Q

What can affect alpha helix stability

A

Interactions between R groups

17
Q

Describe the beta conformation

A

Backbone of PP is extended in zigzag structure with chains arranged side by side and linked by H bonds, adjacent segments can be from the same or different PP chains and can be parallel or anti parallel to eachother

18
Q

What is a beta sheet

A

Arrangement of several segments side by side all in beta conformation

19
Q

What is the difference in the tertiary structure to the primary and secondary

A

Tertiary is overall 3D structure and has lower range effects such as folds in chains that may cause interactions between AA residues far apart in the polypeptide

20
Q

What are the 3 main classes of quaternary structures

A

Fibrous, globular and intrinsically disordered

21
Q

Describe fibrous proteins

A

Extended PP chains with usually one type of secondary structure, Insoluble in water and relatively simple tertiary structures

22
Q

Describe globular proteins

A

Folded PP chains often with several types of secondary structure and a complex tertiary structure

23
Q

What is the function of fibrous proteins

A

Provide structural support to cells and tissues

24
Q

Give two examples of important fibrous proteins

A

alpha keratin and collagen

25
Q

Describe alpha keratins properties

A

Very strong coiled-coil protein, 2 alpha helices intertwined to form a coiled- coil super helix

26
Q

Where is alpha keratin found

A

Mammal’s hair, wool, nails, hooves and outer layer of skin

27
Q

What are the properties of collagen

A

3 helical chains each nearly 1000 residues with 3 AA residues per turn (unlike alpha helixes) , every third residue is glycine (smallest AA) so the interior is very crowded, three chains wind together to form triple stranded superhelical cable stabilised by H bonds

28
Q

Where is collagen found

A

Skin, bone, tendon, cartilage and teeth

29
Q

What type of protein is myoglobin

A

Globular

30
Q

What are the functions of myoglobin

A

Oxygen binding protein in muscle cells, Stores O2 and facilities diffusion in muscle tissue

31
Q

What are the properties of myoglobin

A

Relatively small, single PP chain, 153 AA residues , prosthetic group, contains heme, interior contains almost entirely nonpolar residues hidden from exposure to water, exterior is mostly charged and polar side groups of AAs that interact with water molecules

32
Q

What is a dimer

A

A protein with 2 subunits

33
Q

What is an oligomer

A

Protein with a few subunits

34
Q

What are the properties of human haemoglobin

A

A tetramer with two identical subunits of one type ( 2 alpha subunits and two beta subunits)

NUT1004 (14 decks)

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