Lecture 2 Flashcards

Proteins (33 cards)

1
Q

What structure do proteins of the leucine-rich receptor class adopt?

A

A curved structure

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2
Q

What is a protein secondary structure solely due to?

A

Backbone hydrogen bonding

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3
Q

Describe alpha amino acids.

A

only one carbon atom separates the amino group from the carboxylic acid group (attached to the same carbon).

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4
Q

Are amino acids chiral?

A

Yes

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5
Q

What are the free ends of the linear chain of a protein chain denoted as?

A

Amino terminus (N-terminus) - where free amino group is located, and carboxy terminus (C-terminus) - where the free carboxylic acid group is located

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6
Q

What makes a residue?

A

when a free amino acid is incorporated into a protein chain

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7
Q

What gives each protein its unique structural and functional properties?

A

Side chains

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8
Q

What is the backbone of the protein made up of?

A

Atoms that form the peptide bonds, N-terminus, C-terminus

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9
Q

What does Ca represent?

A

Alpha carbons of the two amino acid residues linked by the peptide bond

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10
Q

What are the consequences of the peptide bond’s partial double bond character? (3)

A

No free rotation about the peptide bond (w), Two alpha carbons (Ca) are usually trans to each other, and The six backbone atoms about each peptide bond (C, O, N, H) are coplanar

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11
Q

Why do peptide bonds usually have trans geometry?

A

For stability of the molecule

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12
Q

Can rotation occur anywhere besides the peptide bond?

A

Rotation can occur at psi and phi, but may be sterically hindered

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13
Q

What would make up a forbidden psi and phi combination?

A

Steric crowding between main-chain atoms - tripeptide

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14
Q

What is an allowed psi and phi combination?

A

Dipeptide - two amino acid residues linked by a peptide bond - Hold one bond angle fixed, Rotate the other bond through a given angle.

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15
Q

How are permitted combinations determined?

A

Computational tools or modelling kits

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16
Q

What is the Ramachandran plot?

A

A map of all theoretically possible combinations of psi and phi angles

17
Q

What makes up hydrogen bond length?

A

The distance between the electronegative donor and acceptor atoms

18
Q

Are covalent bonds stronger than hydrogen bonds?

A

Yes, 10 to 100 times stronger

19
Q

What results in attraction vs. repulsion

A

attraction if opposite charge, repulsion if they have the same charge

20
Q

What was determined before the first protein was?

A

men predicted the existence of secondary structures: repeat structural patterns formed due to repeat hydrogen bonding patterns in the protein main chain.

21
Q

Primary structure

A

amino acid sequence of the chain - Linear sequence of amino acid residues in the protein chain

22
Q

Secondary structure

A

arises from backbone H-bonding in the chain

23
Q

Tertiary structure

A

folding of the secondary structures, involving side chains

24
Q

Quaternary structure

A

Arises with multichain proteins.

25
What is the formula for where H-bonds are formed?
n + 4
26
What is the helix translation?
the distance moved along the helix per residue
27
What is the pitch of the helix?
Length per turn
28
Where are H-bonds on an alpha helix?
co-linear with the chain direction
29
Where are H-bonds on beta sheets?
at nearly right angles to the direction of the chain, and are between at least two strands
30
What is the difference between the resulting structure in parallel strands & antiparallel strands?
Parallel strands tend to give flatter extended sheets, Antiparallel strands have a slight twist and can form barrel-like structures
31
On the basis of mass, which is most abundant in a living bacterial cell?
Water
32
Covalent bonds are formed by the sharing of electrons. In the cell, how are covalent bonds broken?
by enzyme catalysis that is specific for a protein and its substrate
33
How do protein, nucleic acid, and polysaccharide molecules polymerize (grow in length)?
Condensation reactions