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Bcem 431 > Lecture 1 > Flashcards

Lecture 1 Flashcards

1
Q

What is the strongest types of bond?

The weakest

A

Covalent

Van der waal

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2
Q

What’s a salt bridge

A

A interaction between a positive to negative molecule

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3
Q

When is a protien active

A

When its folded (3d)

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4
Q

What did J. sumner show

A

He crystallized the protien urase then redissovled it

The activity of the protien stayed the same meaning ta structure inside the crystal was the same as in solution

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5
Q

How are peptide bonds formed

A

The c of COOH gets attacked by the nitrogen of the other amino acid

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6
Q

What is special about the equilibrium of amino acids

A

The broken peptide bond is more favourable so we need a catalyst like a ribosome to form the peptide bond and make the reaction go the other way

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7
Q

What is omega

Phi

Psi

A

Tell if protien is trans or cis around the peptide bond (180 trans 0 cis)

Rotation in c aplha and n

Rotation in c alpha and c=o

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8
Q

Regions of the ramachandran plot and the protien structure in each region

A

Anti para beta

Para beta

Triple helix (collagen)

Right twisted beta sheets/right handed alpha helix

Left handed alpha helix

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9
Q

What is special about glycine and proline in terms of the angles and ramachandran

A

The glycine has less restrictive structure because of the lack of side chain

So it takes up more area in the plot because it can do more angles

Proline is more restricted because of its rings

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10
Q

Proline and glycine are

A

Helix breaking

They are not favoured in a helix and actual are at the end of them

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11
Q

Valine and Leucine are

A

Favoured in membrane protiens because they are hydrophobic, the don’t make h bonds in the aplha helix with other aa

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12
Q

How does alpha helix get formed

A

Through h bonding between amino acids

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13
Q

What is special about beta sheets compared to alpha helix

What does this mean

A

The distance between adjacent aA in the sheet is 3.5 A

It’s 1.5 in alpha helix

Beta sheets are less compact than helices

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14
Q

What are loops and turns

A

Type of secondary structure that can be rigid or flexible

Antibody bind to these loops and turns

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15
Q

Which type of loops/turns are prolines favours in

A

Short rigid ones because of small ring side chain

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16
Q

What are the types of secondary structures

A

Helix

Beta sheet

Loops/turns

17
Q

What are soluble protiens

What type of protien is the exception to being soluble

A

They are folded into compact structures with non polar cores

Membrane protiens, the have nonpolar cores but are not soluble

18
Q

What is protien folding driven by

A

The hydrophobic effect

More in rec slide 27

19
Q

What is a motif

A

A sequential motif is a sequence in a protein that is repeated

Ex. Pxxp repeating

20
Q

Tertiary structure is

A

Polypeptide chain

21
Q

Quaternary structure is

A

Assemble polypeptide chains (ex. Tetramer)

Bcem 431 (26 decks)

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