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AH Biology > 1.2 Proteins > Flashcards

1.2 Proteins Flashcards

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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?

A

Lysosomes

25
Q

Which organelle is a series of flat membrane discs that helps to package molecules to be moved out of the cell?

A

Golgi Apparatus

26
Q

What are the functions of the non-coding regions of DNA?

A

Making rRNA, making tRNA, Protection

27
Q

Once proteins are made in the ER, how are they transported to other places in the cell?

A

Vesicles

28
Q

Which molecule controls post-translational modification?

A

Enzymes

29
Q

What are functions of the microtubules?

A

Provide structure and shape, moving proteins to other membranes

30
Q

Complete the sentence: “binding sites must have a complimentary ______ and _______”

A

Shape

Chemistry

31
Q

What is an example of a secreted protein?

A

Hormones, Digestive enzymes

32
Q

Once proteins have been made on the RER, where do they go next?

A

Lumen of the RER

33
Q

Many secreted proteins are synthesised as inactive precursors and must be changed to become active proteins. What is this change called?

A

Proteolytic Cleavage

34
Q

What determines protein structure?

A

Amino Acid Sequence

35
Q

What part of amino acids make them differ from each other?

A

R-Groups

AH Biology (10 decks)

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