Proteins And Amino Acids Flashcards

(28 cards)

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

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
What do proteins want to achieve when folding?
Finding the most stable conformation
26
Why are some amino acid side chains charged at physiological pH?
They contain a carboxylic acid or an amine group
27
What does the pKa value of an amino acid side chain tell you about that chemical group?
How likely the side chain will become deprotonated When pH=pKa there are equal numbers of protonated and unprotonated groups
28
What is the relationship between pH and pKa?
pH > pKa = acidic, proton donor pH < pKa = basic, proton acceptor