1.6 Proteins Flashcards

(30 cards)

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
Shape of globular proteins
Spherical, glob shape
24
Solubility of globular proteins, why?
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
Name the 4 types of body proteins
Structural proteins, enzymes, antibodies, hormones
26
Describe the structure of antibodies
Globular proteins: Two pairs of polypeptide chains eg 2 long and 2 short
27
What do channel proteins do How does its structure relate to its function
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
Where is collagen found
Tendons: which join muscles to bones