Proteins And Amino Acids Flashcards

1
Q

What are sequences of amino acids encoded by?

A

A gene

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2
Q

How are amino acids classified?

A

According to chemical properties of the R groups

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3
Q

What determines the acid-base behaviour?

A

R groups

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4
Q

What are the components of an amino acid?

A

Amino group
Carboxyl group
H atom
R group

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5
Q

What is a zwitterion? Why is it most common? One property

A

Net charge of 0 - equal number of positively and negatively charged ions
Most stable
Acts as an acid and a base

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6
Q

Two ends of a polypeptide chain

A

Amino terminal (NH3+)
Carboxyl terminal (COO-)

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7
Q

What is the acid base behaviour determined by?

A

The R group

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8
Q

What is an amino acid residue?

A

Amino acid after it has formed a peptide bond with another amino acid

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9
Q

Chemical properties of R groups

A

Hydrophobic/philic
Polarity
Acid or Base

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10
Q

What are the two categories of R groups

A

Aliphatic - only C and H
Aromatic - phenyl ring

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11
Q

What is a peptide bond?

A

Linking two amino acids
Removing a water molecule

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12
Q

What is an amino terminus and Carboxyl terminus?

A

+NH3
COO-

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13
Q

What is the shape of a peptide bond and what does it mean?

A

Planar
On the same plane

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14
Q

What is the central C called?

A

C alpha

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15
Q

What is a key characteristic of a peptide bond?
What property does this give it?

A

Partial double bond characteristic between the C and N

Very rigid

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16
Q

Does a peptide have a cis or trans configuration?
Describe it

A

Nearly always trans

Cs on opposite sides of C-N bond

17
Q

What are Psi and Phi bonds?
What can they do?
What does this allow?

A

C alpha - C
C alpha - N

Rotate around the peptide bond

A 3D shape

18
Q

Define the isoelectric point

A

The pH at which there is no overall net charge

19
Q

What stabilises the alpha helix?

A

H bonds between the N-H and C=O

20
Q

What is the direction of the alpha helix

A

Right handed

21
Q

What are beta sheets composed of?
What is there parallelilty?
What are the bonds?

A

Adjacent B strands - can be parallel or anti parallel
Stabilised by H bonds between the H on NH and O on C=O

22
Q

Two comparisons between globular and fibrous proteins

A

G - compact F - extended
G - several types of secondary structures F - single type of repeating secondary structure

23
Q

How do polypeptide chains fold in relation to hydrophobic and hydrophilic regions?
Why>

A

Hydrophobic side chains inside

Charged, hydrophilic regions can interact with aqueous solutions

24
Q

Describe quaternary structures

A

Non covalent bonds between complementary hydrophobic and hydrophilic sub units - doesn’t have to be proteins

25
Q

What do proteins want to achieve when folding?

A

Finding the most stable conformation

26
Q

Why are some amino acid side chains charged at physiological pH?

A

They contain a carboxylic acid or an amine group

27
Q

What does the pKa value of an amino acid side chain tell you about that chemical group?

A

How likely the side chain will become deprotonated
When pH=pKa there are equal numbers of protonated and unprotonated groups

28
Q

What is the relationship between pH and pKa?

A

pH > pKa = acidic, proton donor
pH < pKa = basic, proton acceptor