Protein Structure and Function Flashcards

1
Q

Protein function is affected by what

A

Conformations (shape of protein)

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2
Q

Protein structure can be defined at what 4 levels?

A

-Primary: sequence of amino acids
-Secondary: formation of a coil or sheet
-Tertiary: all coils/sheets together
-Quaternary: interaction of one or more polypeptides to form a functional protein

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3
Q

Amino acids in a polypeptide are connected by what

A

Peptide bonds

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4
Q

How many amino acids are used to form polypeptides

A

20

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5
Q

Amino acids within a polypeptide can form noncovalent interactions that cause the polypeptide to do what?

A

The polypeptide folds

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6
Q

The interactions of amino acids with each other leads to a what level of protein structure

A

The 2 degree structure

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7
Q

What is secondary structure determined by

A

Energetic considerations

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8
Q

In a secondary structure free energy is minimized so it is ________

A

Energetically favorable

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9
Q

Noncovalent interactions can be broken, causing the structure to unfold/ denature including what

A

-chemicals
-heat
-pH
-Others

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10
Q

In the tertiary structure, an individual polypeptide chain can have multiple regions of what structure

A

Secondary structure

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11
Q

tertiary structure is the full 3D conformation of the polypeptide including

A

-helices
-sheets
-loops
-and other folds

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12
Q

All polypeptides will have

A

1 degree, 2 degree, and 3 degree structure

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13
Q

Some 3 degree structures are functional ________

A

By themselves

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14
Q

What can 3 degree polypeptide structures do before a functional unit (protein) occurs

A

interact with other 3 degree polypeptide structures

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15
Q

The interaction of two or more 3 degree polypeptides structures is what

A

4 degree structure

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16
Q

Quaternary structure is a complex of two or more __________

A

Polypeptide chains

17
Q

Does it matter if the polypeptides interacting with one another are the same or different?

A

No they can be either the same or different

18
Q

Is protein structure related to function

19
Q

All proteins bind to what

A

other molecules

20
Q

What is a binding site?

A

where a ligand binds a protein

21
Q

Are the interactions at protein binding sites covalent or noncovalent

A

non covalent and specific

22
Q

binding the ligand changes what

A

The protein conformation

23
Q

One the ligand is binded and the protein conformation occurs, what happens

A

Activation or inactivation of a protein

24
Q

What are enzymes

A

Proteins that catalyze chemical reactions

25
Do enzymes make reactions occur faster?
Yes, 1,000,000
26
Enzymes hold substrates in ways that allows chemical reactions to occur more easily that does what
Reduces activation energy
27
Different mechanisms for reducing activation energy depends on what
The enzyme
28
What are 5 ways that protein activity is controlled
-feedback inhibition -multiple binding sites -phosphorylation -GTP-binding -ATP hydrolysis
29
Anabolic pathways produce what for the cell
organic compounds
30
What are protein kinases
enzymes that add phosphates to other proteins
31
What are protein phosphatases
Removes phosphates from other proteins
32
What kind of enzymes have more than one binding site and are active or inactive based on what is bound
allosteric enzymes
33
ATP binding and ATP hydrolysis causes what type of change in a protein
Conformational change
34
Motor proteins are involved in what
muscle contractions and transport of materials in cells
35
GTP is what
Nucleotide triphosphate
36
When the GTP is hydrolyzed what happens to the protein
the protein is inactivated
37
Protein is reactivated when
GTP binds again
38
Phosphorylation may do what to the protein
activate or inactivate