1.2 Proteins Flashcards

(35 cards)

1
Q

What is the proteome?

A

The proteome is the entire set of proteins expressed by a genome

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2
Q

Why is the proteome larger than the genome?

A

More than one protein can be produced from a single gene as a result of alternative RNA
splicing

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3
Q

What is the primary structure of a protein and what type of bond is it made from?

A

A sequence of a chain of amino acids that have bonded through a condensations reaction.
Bonding: peptide bond

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4
Q

What is the secondary structure of a protein?

A

Structure: Alpha helix and Beta sheets
Bonding: hydrogen bonds

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5
Q

What is the tertiary structure of a protein?

A

Hydrophobic side chains folded inwards

Bonding: disulphide bridges, ionic bonds, LDFs, hydrophobic interactions

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6
Q

What is the quaternary structure of a protein?

A

More than one polypeptide chain bonded together.

Can also have sub-units attached

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7
Q

Where does post translational modification take place and what are the forms of post translational modification?

A

Where: in the golgi

Forms of modification: addition of chemical groups, covalent modification

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8
Q

Name the 4 amino acid group categories and describe them

A

basic - positively charged
acidic - negatively charged
hydrophilic/polar - is attracted to water
hydrophobic/non-polar - isn’t attracted to water

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9
Q

What is the RER and how does it differ from the SER?

A

RER is covered in ribosomes

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10
Q

Describe the translation of the cytosolic proteins and secreted proteins

A

cytosolic protein - translation on cytosolic ribosomes

secreted proteins- translated on ribosomes on RER

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11
Q

Describe the pathway of a secreted protein?

A

Protein enters RER lumen, move in vesicles to Golgi apparatus, post translational modification, packaged in secretory vesicles, fuse with plasma, move along microtubules

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12
Q

What is a ligand?

A

A ligand is a substance that can bind to a protein

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13
Q

What are modulators?

A

Modulators bind with the allosteric site and bring about conformational change

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14
Q

What are negative modulators?

A

Negative modulators lock the enzyme into an inactive form i.e. decreasing the enzyme affinity for the substrate

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15
Q

What are positive modulators?

A

Positive modulators lock the enzyme into active form i.e. increases the enzyme’s affinity for the substrate

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16
Q

What are kinases?

A

Kinases add a phosphate group (phosphorylates)

17
Q

What are phosphatases?

A

Phosphatases remove a phosphate group (dephosphorylates)

18
Q

Which factors can affect the interactions between R-Groups?

A

Temperature, light

19
Q

What type of covalent bond between R-groups containing sulfur?

A

Disufide bond

20
Q

What is the name for a non-protein unit tightly bound to a protein?

A

Prosthetic group

21
Q

Which organelle is the site of transmembrane protein synthesis?

A

Rough Endoplasmic Reticulum (RER)

22
Q

Which organelle is the site of cytosolic protein synthesis?

A

Cytosolic Ribosomes

23
Q

Which organelle is the site of lipid synthesis?

A

Smooth Endoplasmic Reticulum (SER)

24
Q

Which organelle contains hydrolases that digest protein, lipids, nucleic acids and carbohydrates?

25
Which organelle is a series of flat membrane discs that helps to package molecules to be moved out of the cell?
Golgi Apparatus
26
What are the functions of the non-coding regions of DNA?
Making rRNA, making tRNA, Protection
27
Once proteins are made in the ER, how are they transported to other places in the cell?
Vesicles
28
Which molecule controls post-translational modification?
Enzymes
29
What are functions of the microtubules?
Provide structure and shape, moving proteins to other membranes
30
Complete the sentence: "binding sites must have a complimentary ______ and _______"
Shape Chemistry
31
What is an example of a secreted protein?
Hormones, Digestive enzymes
32
Once proteins have been made on the RER, where do they go next?
Lumen of the RER
33
Many secreted proteins are synthesised as inactive precursors and must be changed to become active proteins. What is this change called?
Proteolytic Cleavage
34
What determines protein structure?
Amino Acid Sequence
35
What part of amino acids make them differ from each other?
R-Groups