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
what is a tertiary structure due to?
interactions between the R groups
26
what is a quaternary structure
when protein has more than one polypeptide sub-unit
27
what is the function of an enzyme and give an example?
catalysis of bond breaking and bond making. e.g. amylase
28
what is the function of structural proteins and give an example?
provides mechanical support of cells and tissues. e.g. collagen
29
what is the function of a transport protein and give an example?
carries small molecules and ions. e.g. haemoglobin
30
what is the function of a motor protein and give an example
generates movement in cells and tissues. eg. myosin in skeletal muscle
31
what is the function of a storage protein and give an example
stores small molecules and ions. e.g. iron
32
what is the function of a signalling proteins and give an example
carries signals from cell to cell. eg. insulin
33
what are receptor proteins and give an example
detect signals and transmit to cell's response machinery. eg. insulin receptor
34
what is a gene regulatory protein and give an example
bind to DNA to switch on or off genes. e.g. repressor protein in lac operon
35
what is the isoelectric point of a protein?
pH at which the protein has no overall charge