Chapter 3: Protein structure and function Flashcards

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1
Q

These proteins are involved in the response of a cell to a chemical stimulus

A

receptor proteins

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2
Q

These are responsible for almost everything an organism does and they are structurally diverse and have a wide range of functions as a result

A

Proteins

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3
Q

What is a prion?

A

Infectious proteins that can also cause normal proteins to misfold. They can’t be treated and can be acquired through ingestion.

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4
Q

How important is one amino acid in a protein?

A

If one amino acid is changed in a protein it depends if it will have an effect or not

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5
Q

What is a polymer constructed from amino acids that haven’t been folded called?

A

Polypeptide

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6
Q

What occurs in the backbone in the secondary protein structure?

A

Hydrogen bonding

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7
Q

These proteins are responsible for movement

A

contractile and motor proteins

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8
Q

What are the amino acids with electrically charged side chains?

A

Aspartate, glutamate, lysine, arginine, histidine

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9
Q

What is the core structure to all amino acids?

A

Amino group, carboxyl group, C-H, and an R-group

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10
Q

What is the name of a polypeptide that has folded?

A

Protein

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11
Q

The fourth level of protein structure in which multiple polypeptides come together. It is not found in all proteins

A

Quaternary

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12
Q

These proteins accelerate chemical rxns necessary to sustain life

A

enzymatic proteins

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13
Q

What are the beginning and ends of a polypeptide called in the residue numbering system?

A

N-terminus = beginning

C-terminus = end

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14
Q

How are peptide bonds formed?

A

Dehydration/condensation reaction

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15
Q

These proteins store amino acids

A

storage proteins

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16
Q

What do some proteins require to fold properly?

A

Molecular chaperones

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17
Q

What are amyloid diseases?

A

A build up of misfolded proteins

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18
Q

These proteins transport substances

A

transport protein

19
Q

What types of things can alter protein folding?

A

Environment. Temperature, pH, etc.

20
Q

These proteins help with support

A

structural proteins

21
Q

Where do peptide bonds form?

A

Between a carboxyl group and an amino group, thus linking the carbon from the carboxyl to the nitrogen of the amino group

22
Q

The third level of protein structure in which there are interactions between R groups. Most proteins stop here

A

Tertiary

23
Q

These can only occur at certain points in protein folds and can’t just occur anywhere on the polypeptide

A

Alpha helix and Beta pleated sheets

24
Q

The second level of protein structure where hydrogen bonds between amino and carbonyl groups in backbone. Forms alpha helicies and beta pleated sheets

A

secondary

25
Q

Can a protein function in its primary structure?

A

No, it’s also technically still a polypeptide as no folding has occurred

26
Q

What is the bond called that links amino acids together?

A

Peptide bond

27
Q

Eight different protein types

A

Enzymatic, defensive, storage, transport, hormonal, receptor, contractile and motor, and structural

28
Q

What diseases are associated with misfolded proteins?

A

Amyloid diseases like Alzheimer’s, Parkinson’s, ALS, Type II Diabetes, and Bovine Spongiform Encephalopathy (Mad cow disease)

29
Q

These proteins protect against disease

A

defensive proteins

30
Q

What are the monomers of proteins?

A

amino acids

31
Q

These account for more than 50% of the dry weight of our bodies

A

Proteins

32
Q

What determines the primary structure of a polypeptide and why?

A

The DNA sequence of that gene because DNA has directions for making proteins

33
Q

What is the sequence of central atoms a polypeptide that hasn’t folded follows?

A

N-C-C-N-C-C-N-C-C-N…

34
Q

These proteins help in coordination of an organisms activities

A

hormonal proteins

35
Q

What are the two types of folds a polypetide/protein can make that we need to know?

A

Alpha helix and Beta pleated sheets

36
Q
A

Amino acid. Amino group on left side. Carboxyl group on ride side.

37
Q

In this structure, side chains start interacting with each other

A

Tertiary structure

38
Q

The first level of protein structure in which there is a chain of amino acids

A

primary

39
Q

What are the amino acids with polar side chains?

A

Serine, threonine, tyrosine, asparagine, and glutamine

40
Q

How does sickle-cell anemia form?

A

In the primary structure of the protien, Glu-6 changes to Val-6. This one change in amino acids causes the difference in red blood cells

41
Q

What are the amino acids with nonpolar side chains?

A

Glycine, alanine, valine, leucine, isoleucine, methionine, cysteine, phenylalinine, tryptophan, and proline

42
Q

What is the longest protein and how long is it?

A

Titin (connectin) and it is 34350 amino acid residues long

43
Q

In this structure, two or more polypeptides come together

A

Quanternary structure

44
Q

What are the 4 levels of protein structure?

A

Primary, secondary, tertiary, and quaternary