1.6 Proteins Flashcards

1
Q

What are amino acids

A

Basic monomer units which combine to make up a polymer called a polypeptide.

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1
Q

What can polypeptides be combined to make

A

A protein

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2
Q

How many amino acids occur naturally in protein

A

20 out of 100 amino acids

These 20 amino acids occur in all living organisms- which provides evidence for evolution

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3
Q

Each amino acid has a central carbon atom which connects to four different chemical groups

What are they

A

. An amino group (-NH2)
Basic group that gives it its name

. Carboxyl group (-COOH)
Acidic group which makes it acidic

. Hydrogen atom (-H)

. R group
Which Is a variety of different chemical groups. Each amino acid has a different R group
. Amino acids only differ in their R groups

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4
Q

What bond is formed between amino acid monomers to form a dipeptide

A

Peptide bond

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5
Q

What type of reaction is it when a dipeptide is formed

A

. Condensation reaction: a molecule of water is removed from the reaction

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6
Q

How is the water molecule made from amino acids bonding

What bond forms between them

A

Condensation reaction:

The OH from carboxyl group of one amino acid and a H from the amino group of another amino acid

A peptide bond forms between them

These make H2O

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7
Q

How can the peptide bond be broken

A

Hydrolysis, adding a molecule of water , to give two constituent amino acids

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8
Q

What is the primary stage of proteins

A

Polypeptides:

. Amino acid monomers joined together in polymerisation

. The sequence of amino acids in a polypeptide chain forms primary structure of any protein

====================

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9
Q

Why are there many types of primary protein structure

A

. The 20 naturally occurring amino acids join in different sequences so there are loads of possible combinations

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9
Q

What does the primary structure of a protein determine

A

. It ultimate shape and hence its function

. A change in a single amino acid in the primary sequence can change the shape of the protein stop it carrying out its function

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10
Q

What is the secondary structure of proteins

A

. Linked amino acids that make up polypeptides possess both NH and -C=O groups.

These groups have opposite charges due to oxygen having - charge and H having + charge

. These groups form hydrogen bonds

\ \ / /\ \ / /\ \
\ \ / / \ \ / / \ \
\ \/ / \ \ / / \ \
\/ \/ \ \
The shape can be an alpha helix or beta sheets, but both are formed by hydrogen bonds

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11
Q

What do the hydrogen bonds on secondary structure of proteins cause

A

Cause long polypeptide chain to be twisted into a long 3D shape like the coil on an alpha helix

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12
Q

What is the tertiary structure of proteins

A

The alpha helixes of secondary protein can be twisted and folded even more to give complex 3D structure of each protein

This structure is maintained by a number of different bonds. Where the bonds occur depend on the primary structure

Looks like a knot a bit

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13
Q

What 3 types of bonds are found on tertiary structure

A

. Disulphide bridges: Fairly strong and not easily broken

. Ionic bonds: Formed between carboxyl and amino groups that aren’t involved in forming peptide bonds.
They’re weaker than disulphide bonds and are easily broken by changes in PH

.Hydrogen bonds: Numerous but easily broken

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14
Q

What is the quaternary structure of proteins

A

Large proteins form complex molecules containing lots of individual polypeptide chains linked in various ways.

There can be non proteins (prosthetic groups) associated with the molecules also

15
Q

How do you test for proteins

A

Biuret test: Detects peptide bonds

. Place a sample of the solution to be tested in a test tube and add an equal volume of sodium hydroxide solution at room temp

. Add a few drops of dilute copper sulfate solution, and mix gently

. Purple colouration indicates peptide bonds being present, and hence a protein

If no protein is present solution remains blue

16
Q

What function do fibrous proteins have

Give the example

A

. Eg collagen, have structural functions

17
Q

Structure of fibrous proteins

A

. Form long chains which run parallel to each other so cross bridges link them together.
This makes them very stable

18
Q

What is the primary structure of collagen

A

. Unbranched polypeptide chain

19
Q

Secondary structure of collagen

A

. Polypeptide chain is very tightly wound

The amino acid glycine is present as every 3rd amino acid helps tight packing

20
Q

Tertiary structure of collagen

A

. Chain is twisted into a second helix

21
Q

Quaternary structure of collagen

A

. Made up of 3 polypeptide chains wound together in the same way as individual fibres are wound together in a rope

Hydrogen bonds keep it together

22
Q

What are globular proteins

A

Eg enzymes and haemoglobin carry out metabolic functions

23
Q

Shape of globular proteins

A

Spherical, glob shape

24
Q

Solubility of globular proteins, why?

A

Soluble in water

Because some amino acids have hydrophilic R groups that are attracted to water

. They have hydrophilic amino acids on their surface, so they interact with water molecules

The hydrophobic amino acids are in the centre of the protein, away from water

25
Q

Name the 4 types of body proteins

A

Structural proteins, enzymes, antibodies, hormones

26
Q

Describe the structure of antibodies

A

Globular proteins: Two pairs of polypeptide chains eg 2 long and 2 short

27
Q

What do channel proteins do

How does its structure relate to its function

A

Its primary function is to transfer ions and water molecules through the membrane:
Involved in substances entering and leaving the cell

It has a hydrophilic and a hyrophobic side so one side attracts water nd the other repels water.
This allows the protein to fold up and form a channel through the cell membrane where the water soluble molecules can pass through

28
Q

Where is collagen found

A

Tendons: which join muscles to bones