1.23 a) Protein Structure Flashcards

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1
Q

The distinguishing features of protein molecules are the __ nature and their ability to ___ to other molecules.

A

folded, bind

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2
Q

Proteins are made of ___ ___.

A

amino acids

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3
Q

The amino acid sequence determines the ___ ___ and is held together by ___ ___.

A

protein structure, peptide bonds

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4
Q

A peptide bond is a chemical bond that forms between two amino acids when the ___ group of one molecule and the ___ group of another react, releasing a ___ molecule.

A

amino, carboxyl, water

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5
Q

The _ groups of amino acids are responsible for the unique characteristics of ___ and often interact with other ___

A

R, proteins, molecules (eg integral/peripheral membrane proteins interacting with phospholipids, binding them to the membrane)

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6
Q

The R groups of amino acids vary in s__, s__, c__, c__ r__, and h__ b__ c__.

A

size, shape, charge, chemical reactivity, and hydrogen bonding capacity

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7
Q

There are four groups of amino acids, which are classified by their R groups. Name them please.

A

Acidic,
Basic,
Polar,
Hydrophobic.

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8
Q

Describe the four types of amino acids/R groups.
Acidic is ___.
Basic is ___.
Polar is ___.
Hydrophobic is ___.

A

acidic is negative,
basic is positive,
Polar is hydrophilic,
hydrophobic is non-polar.

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9
Q

The wide range of functions carried out by proteins is a result of the ___ of _-___.

A

Diversity, R-groups

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10
Q

The structure of a polypeptide has (how many?) ___ divisions, each combining to make a unique ___.

A

four, protein

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11
Q

The primary structure of a polypeptide is…

A

the order of amino acids in the polypeptide chain

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12
Q

The secondary structure of a polypeptide is…

A

The hydrogen bonding along the backbone

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13
Q

The hydrogen bonding of secondary structure can fold the polypeptide into ___ ___, ___ ___ or ___.

A

Alpha helices, beta sheets, turns

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14
Q

The alpha helices look like ___ stranded RNA.
The beta sheets can be ___ or __-___.

A

single.
parallel, anti-parallel

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15
Q

The tertiary structure of a polypeptide is when the ___ polypeptide is ___.

A

entire, folded

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16
Q

The polypeptide’s folds in tertiary structure can be stabilised by five different forces between R groups. Name them please.

A

Disulfide bridges,
hydrogen bonds,
ionic interactions,
hydrophobic interactions,
LDFs

17
Q

The quarternary structure of a polypeptide is the ___ arrangement of multiple ___.

A

spatial, polypeptides

18
Q

The quarternary structure of a polypeptide only exists in proteins with ___ than one ____ ___.

A

more, polypeptide chain

19
Q

What is a prosthetic group?
Give me an example please.

A

A non-protein component of a protein that is required for its function
Haem groups in haemoglobin (they are what enables haemoglobin to bind to oxygen)

20
Q

Two factors that affect the interactions between R groups are ___ and __. If conditions are too extreme, the forces of the ___ structure will break, un-folding and denaturing the ___.

A

temperature and pH.
tertiary, protein

21
Q

pH changes can disrupt the interactions between what two types of R group?

A

acidic, basic

22
Q

If the pH value is ever too far from the ___ value, the ___ interactions between charged R groups is lost, causing the protein to ___.

A

optimum, ionic, denature