Chapter 5- Biochemistry (1) Flashcards

1
Q

Give some functions of proteins:

A

1- Proteins come in the form of enzymes

2- Can be used for transport and storage, i.e, haemoglobin

3- Mechanical support

4- Signalling and receptors

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2
Q

What do amino acids contain?

A

1- A central C that forms 4 single covalent bonds to

2- Amino group (NH2)

3- Carboxyl group (COOH)

4- H atom

5- R group- variable unit and determines what type of amino acid and determines the chemical nature of that amino acid

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3
Q

How many standard amino acids are there?

A

20

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4
Q

The different chemical properties are:

A

1- Acidic
2- Basic
3- Non- polar
4- Polar

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5
Q

What is the formation of proline?

A

The R group covalently binds to the NH2 group of the central carbon which folds back the amino acid.

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6
Q

What makes proline different to other amino acids?

A

It has more rigidity compared to other amino acids

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7
Q

What does the rigidity of proline help stabalise?

A

Folded proteins

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8
Q

Where is proline often found?

A

Often found in very tight turns in protein structures, where the polypeptide chain must change direction.

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9
Q

How are amino acids held together?

A

Amino acids are held together by peptide bonds.

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10
Q

What is a dipeptide?

A

Two amino acids joined together

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11
Q

What is a polypeptide?

A

Two or more amino acids joined together

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12
Q

When amino acids join together, what reaction takes place?

A

Condensation reaction

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13
Q

What is a condensation reaction?

A

When two molecules join together and release water.

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14
Q

How is the protein shape dictated?

A

By the amino acid sequence

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15
Q

What bonds never form between R groups?

A

Covalent bonds

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16
Q

What is a disulphide bond?

A

Disulphide bond- covalent links between the sulphur atoms of two cysteine amino acids.

17
Q

Secondary protein structures include:

A

Alpha- helix- rod like structure or coil that has a single polypeptide chain

Beta- pleated sheet- extended polypeptide chains that fold back over each other

18
Q

How is the alpha helix held together?

A

By hydrogen bonds

19
Q

How is the beta pleated sheet formed?

A

Formed by linking two or more beta- strands.

20
Q

In a beta pleated sheet, why is the polypeptide chain fully extended?

A

Because it allows for more hydrogen bonding

21
Q

What are the levels of organisation of protein structure?

A

1- Primary structure- sequence of amino acids

2- Secondary structure- alpha- helix and beta sheet formation with folding as a result of hydrogen bonding between peptides.

3- Tertiary structure- folding of the polypeptide chain. Disulphide bonds form between the R groups of the alpha- helixes and beta sheets.

4- Quaternary structure- complex of several polypeptide chains, e.g, haemoglobin

22
Q

Carbohydrates are what type of polymers?

A

Sugar polymers

23
Q

What do carbohydrates contain?

A

Carbon, hydrogen, and oxygen

24
Q

What is the role of polysaccharides?

A

Polysaccharides serve as compact energy storage molecules (glycogen or starch) or structural elements in plant cell walls (cellulose)

25
Q

What do phosphorylated sugars form?

A

The structural framework of DNA and RNA (ribose).