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Foundations of Medicine > Proteins part 1 > Flashcards

Proteins part 1 Flashcards

1
Q

What is a protein?

A

A protein is a macromolecule consisting of
amino acids arranged in a particular
structure that enables it to carry out a
specific function in a particular context

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2
Q

What are the two types of proteins and their characteristics?

A

Proteins may be structural (e.g. actin
‘scaffold’ within a cell or keratin in skin) or
functional (e.g. catalytic function of
enzymes or antibodies in immune defence)

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3
Q

Steps before protein synthesis (basic )?

A

DNA is both a blueprint and instruction
manual for different proteins
It tells cells how to make messenger
RNA (mRNA)
TRANSCRIPTION
mRNA is used by the cell as a code to
make chains of amino acids
TRANSLATION
These chains go on to form proteins!

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4
Q

What are the nucleotides that make up DNA ?

A

adenine, cytosine, guanine and thymine

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5
Q

Nucleotides that make up mRNA?

A

adenine ,cytosine, guanine and uracil

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6
Q

Describe amino acid structure?

A

always a central carbon atom
always amine group (NH2) on left
carboxylic acid group on the right
always a hydrogen attached to second carbon
has a variable r group

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7
Q

What does an amino acid being chiral mean?

A

distinct orientation in space despite common chemical constitution
-true for all except glycine (R is H )

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8
Q

Why are amino acids affected by acid-base?

A

Have COOH - can lose hydrogen ions
amine group- can behave like a base

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9
Q

What happens when amino acids are subjected to pH?

A

may take on positive or negative charge

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10
Q

What happens to AA in low pH?

A

Lots of H+ ions
carboxylic acid group takes up hydrogen and becomes slightly positive
cation

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11
Q

What happens to AA in high pH?

A

not many h+ ions
carboxylic acid loses hydrogen and becomes slightly negative
anion

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12
Q

Amino acids at pH 7?

A

two charges

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13
Q

What are aliphatic amino acids?

A

R group consisting of hydrocarbon chains
increasing long hydrocarbon - non polar properties

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14
Q

What are aromatic amino acids?

A

r group consisting of hydrocarbon ring

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15
Q

Why are there sulphur-containing amino acids?

A

The presence of sulphur allows interactions called disulphide bridge to form

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16
Q

What are di- sulphide bridges?

A

Covalently bonded linkages that occur between two sulphur containing amino acids and help increase strength

17
Q

What are the acidic amino acids?

A

aspartate and glutamate

18
Q

What are the basic amino acids?

A
  • Lysine
  • Hisitidine
  • Arginine
19
Q

What are polar amino acids?

A

Can carry charge at the end of R group

20
Q

What is the miscellaneous amino acid and why?

A

proline , unusual ring shape- which is very difficult to break

21
Q

Describe primary structure?

A

The sequence in which amino acid monomers are
bonded together to form a polypeptide chain

22
Q

What is a peptide bond?

A

amine and carboxylic acid groups both react together
dehydration reaction

23
Q

What is secondary structure?

A

This is the 3D spatial arrangement of amino acids
located near each other in the polypeptide chain
Relies on hydrogen bonding between the amino
hydrogen of one amino acid and the carboxyl oxygen of another amino acid in the same chain

24
Q

What are the types of secondary structure?

A

alpha helix
and beta pleated sheet

25
Q

Two examples of proteins with spiral alpha helices?

A

troponin - released from myocardium
myoglobin

26
Q

What do troponins tell us?

A

elevations in troponins can help determine if a patient has had a myocardial infarction.

27
Q

What are porin proteins?

A

porin proteins act as channels that allow water into cells

28
Q

What is the tertiary structure?

A

Results when functional groups of ‘R’ chains of amino
acids in the polypeptide chain interact with one another
Van der Waals, ionic, hydrogen, disulphide and
hydrophobic interactions can all be involved
Functional proteins exist as, at least, a tertiary structure

29
Q

What is the quaternary structure?

A

Sometimes several polypeptides interact with one
another to form a quaternary structure

30
Q

Describe structure of haemoglobin?

A

haemoglobin contains four highly-folded
polypeptide chains and four iron-containing heme
groups with one group tucked within the interior of
each folded polypeptide subunit

31
Q

What is denaturation?

A

Occurs when a protein’s chemical bonds are
disrupted (possibly destroyed) within its
secondary and tertiary structure
Biological functionality is LOST
Denaturation processes are rarely strong enough
to break the primary structure of individual
peptide bonds, so the primary structure remains
the same even after denaturation

Foundations of Medicine (27 decks)

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