Unit 1: Proteins Flashcards

1
Q

What are proteins made up of?

A

amino acids

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2
Q

What determines the structure and the function of the protein?

A

The type and order of the amino acids

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3
Q

What is the structure of an amino acid?

A
has a central alpha carbon
an amino group (NH2)
a carboxyl group (COOH)
an R group (variable)
H atom
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4
Q

What is the R group of an amino acid?

A

It is the variable part of the amino acid structure and gives the amino acid unique chemical properties

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5
Q

What are the different R group classifications?

A

Acidic, basic, uncharged polar and non polar

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6
Q

what is an acidic side chain?

A

it is hydrophilic and is COOH group

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7
Q

what is a basic side chain?

A

it is hydrophilic and is NH2/NH3+ group

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8
Q

what is an uncharged polar chain?

A

is it hydrophilic and is OH or CONH2

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9
Q

what is a non-polar side chain?

A

it is hydrophobic and is a hydrocarbon including an aromatic ring

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10
Q

amino acids link together by which bond?

A

a covalent peptide bond

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11
Q

to form a peptide what reaction occurs?

A

condensation reaction between carboxyl group and amino group

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12
Q

what is a residue?

A

amino acids joined by peptide bonds

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13
Q

what bonds apart from peptide bonds are important in protein structure?

A

hydrogen bonds and ionic bonds

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14
Q

what is the primary structure of a protein?

A

the sequence of amino acids in a polypeptide chain

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15
Q

what determines the secondary and tertiary structure of a protein?

A

the primary structure

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16
Q

what are the two main types of secondary structure?

A

alpha helix and beta sheet

17
Q

describe the alpha helix structure

A

polypeptide chain is coiled into a right handed helix held in place by hydrogen bonds between N-H bonds and C=O of another peptide bond

18
Q

describe the beta sheet

A

polypeptide chain linked in a side to side configuration and can be parallel or antiparallel by hydrogen bonds between NH bonds and C=O of another.

19
Q

what is a tertiary structure

A

The way in which a protein folds to give the final protein structure

20
Q

what are van der waals

A

very weak attractions between the electron clouds of atoms

21
Q

what are protein domains?

A

these are produced by any polypeptide chain that can fold independently into a compact, stable structure. protein is mad of one or more domains

22
Q

what is a protein motif?

A

motifs are elements of secondary structure that form in a particular way

23
Q

What is a prosthetic group?

A

final aspect to tertiary structure in proteins is the incorporation of non-protein groups e.g.. iron atom in catalase

24
Q

what is a secondary structure due to?

A

hydrogen bonds between the atoms of the peptide bond

25
Q

what is a tertiary structure due to?

A

interactions between the R groups

26
Q

what is a quaternary structure

A

when protein has more than one polypeptide sub-unit

27
Q

what is the function of an enzyme and give an example?

A

catalysis of bond breaking and bond making. e.g. amylase

28
Q

what is the function of structural proteins and give an example?

A

provides mechanical support of cells and tissues. e.g. collagen

29
Q

what is the function of a transport protein and give an example?

A

carries small molecules and ions. e.g. haemoglobin

30
Q

what is the function of a motor protein and give an example

A

generates movement in cells and tissues. eg. myosin in skeletal muscle

31
Q

what is the function of a storage protein and give an example

A

stores small molecules and ions. e.g. iron

32
Q

what is the function of a signalling proteins and give an example

A

carries signals from cell to cell. eg. insulin

33
Q

what are receptor proteins and give an example

A

detect signals and transmit to cell’s response machinery. eg. insulin receptor

34
Q

what is a gene regulatory protein and give an example

A

bind to DNA to switch on or off genes. e.g. repressor protein in lac operon

35
Q

what is the isoelectric point of a protein?

A

pH at which the protein has no overall charge