Recap amino acids and proteins Flashcards

1
Q

What are the two types of Stereoisomerism ?

A

Geometric Isomerism - rotation prevents double bonding

Optical Isomerism - non- super?. Mirrior image

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2
Q

Explain R groups?

A

The rest of the chain could be anything -i.e.- R groups vary in amino acids

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3
Q

Explain Long straight chain aliphatic?

A

2-3 carbon side makes it hydrophobic

    |   |   |   |
  -c-c-c-c-           Makes molecules
    |   |   |   |.            Makes them twist
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4
Q

What is Amine and Primary amine?

A

Alcohol/hydroxyl - Primary amine has Nitrogen

Amine- Oxygen - important has oxygen

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5
Q

Explain the functional group Alkaline?

A
  • Double bonded, Normal energy’s won’t change configurations
  • Double bond allows us to see RETANIN.
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6
Q

What dose the Phenyl group allow for?

A

Allows for swirl of molecules

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7
Q

Explain the functional group Carboxylic acid?

A
  • Joined with amine makes amino acids - properties of the two keeps PH in body at correct balance (buffers)
  • Can give up hydrogen amine can accept
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8
Q

Explain Geometric Isomerism CIS AND TRANS?

A

When the body wants to respond to a stimuli

Assist groups match TRANS at opposite sides CIS at different sides

Can assist and transfer, single bonds can rotate easily DBL can.

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9
Q

Explain Optical isomers?

A
  • Can change at different temperatures, changes properties of molecules.
  • CHIRAL - mirror images
  • Simple has 4 diff groups attached to a central carbon atom
  • Carbon atom knows as the CHIRAL CENTRE can create an isomer
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10
Q

All amino acids are (L) why?

A

They are all L as sugar tends to be D dees eat L more energy efficient as they won’t have to produce their own L’s

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11
Q

What are proteins for?

A

1) Calalysis for DNA Polymerase
2) Transport - hemoglobin trasports 02 in the body
3) Structure - of collegen( connective-tissue) Keratine in hair nails
4) Motion of muscles i.e. Use of myosin and actin

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12
Q

What are amino acids the right molecule for the functions that proteins need to preform?

A
  • They can form polymers (long chains) can make different shapes from polymers
  • They can act as buffers and regulate PH within the body
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13
Q

What is the structure of Aa’s ?

A

R
| COOH
NH2- CH

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14
Q

What is the R group in Glycine why is it significant?

A

Glycine has a hydrogen atom in the position of an R-group, dose not have a side chain (hydrophilic and non polar)

No chiral centre

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15
Q

Which are the simplest amino acids, which are there side groups?

A

H.
NH2 - CH - COOH

          GLYCINE 

            CH3
              |    NH2 -   CH - COOH

   ALANINE 

BOTH non polar + charged R groups are Methyl and Hydrogen

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16
Q

Name the amino acid which is unique in that the alpha amino group is attached directly to the side chain; forming a ring and making the alpha carbon a direct substituent to the side chain??

A

Proline it helps to form a secondary structure, two folding next to each other could form a beta pleated sheet

17
Q

Why is protein important?

A

Important as it is capable of folding back on its self?

18
Q

What would be the characteristics of an animal acid that is, Aliphatic?

A

R-groups are non polar, hydrophobicity increase its increasing number of C atoms .

19
Q

What would be the characteristics of an amino acid that is polar but uncharged ?

A

Usually hydrophilic, polar functional groups in the side chain

Can form hydrogen bonding with water so capable of interacting with water

20
Q

What would be the characteristics of an amino acid that is, positively charged?

A

Will contain amine groups

21
Q

What would be the characteristics of an amino acid that is negatively charged ?

A

Will contain carboxylic acid groups

22
Q

Draw glycine that has a Acidic PH?

A

H

H2N-CH-COOH

23
Q

Draw glycine with a AlkelinePH ?

A

HN3-CH-COOH.

In acid alkaline will take an acid becoming +

24
Q

Explain Glycine with a Neutral PH?

A

Changes depending on environment it is in

Zwitterion can be + and - charged at the same time

25
Why is the property of amino acids to be ionised differently at different PHs important ?
Important as it can be a buffer
26
What type of bonding occurs in primary structure, the secondary and the tertiary structure ?
Zwitterion bonding
27
What type of bonding occurs in the primary structure of amino acids?
Primary structure is healed together by covalent bonds such as a peptide bonds, they are strong bonds Or the bonding between the amino acid and the carboxylic acid groups gives a condensation reaction
28
What type of bonding occurs in the secondary structure of proteins?
Alpha or B beta pleated sheets, are held together by hydrogen bonds These bonds are easily denatured
29
What type of bonding occurs in the Tertiary structure of proteins?
Vanderval bonding forces bonding between R-groups Ionic bond + and - attract
30
The spiral turn in a alpha helix contains 3.6 residues, why can it be 3 or 4?
Needs 3.6 as it gives the right bonding oxygen can easily bond to hydrogen to form a hydrogen bond .
31
What amino acids, if they appeared next to each other would start to disrupt an alpha helix and instead might be more likely to make the protein form into a beta pleated sheet??
Proline big odd group forces folding