Protein Structure and Function Flashcards

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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

A

yes

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
Q

Do enzymes make reactions occur faster?

A

Yes, 1,000,000

26
Q

Enzymes hold substrates in ways that allows chemical reactions to occur more easily that does what

A

Reduces activation energy

27
Q

Different mechanisms for reducing activation energy depends on what

A

The enzyme

28
Q

What are 5 ways that protein activity is controlled

A

-feedback inhibition
-multiple binding sites
-phosphorylation
-GTP-binding
-ATP hydrolysis

29
Q

Anabolic pathways produce what for the cell

A

organic compounds

30
Q

What are protein kinases

A

enzymes that add phosphates to other proteins

31
Q

What are protein phosphatases

A

Removes phosphates from other proteins

32
Q

What kind of enzymes have more than one binding site and are active or inactive based on what is bound

A

allosteric enzymes

33
Q

ATP binding and ATP hydrolysis causes what type of change in a protein

A

Conformational change

34
Q

Motor proteins are involved in what

A

muscle contractions and transport of materials in cells

35
Q

GTP is what

A

Nucleotide triphosphate

36
Q

When the GTP is hydrolyzed what happens to the protein

A

the protein is inactivated

37
Q

Protein is reactivated when

A

GTP binds again

38
Q

Phosphorylation may do what to the protein

A

activate or inactivate