Bio Hw due 9/15 Flashcards

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1
Q

A polypeptide is a long unbranched chain of

A

Amino acids

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2
Q

The shape of a protein determines its

A

function

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3
Q

Functions of proteins

A
  • they catalyze chemical reactions
  • they transport ions and molecules across the cell membranes
  • provide structural support for many animal tissues
  • play a key role in the contraction of muscles
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4
Q

Proteins are polymers made up of how many different amino acids?

A

20

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5
Q

Which part of an amino acid is ALWAYS acidic?

A

the carboxyl group

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6
Q

the chemical structure of a typical amino acid found in a protein:

A

A central carbon atom is bound to an amino group, carboxyl group, a side chain, and a hydrogen atom.

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7
Q

the 20 common amino acid are classified into 5 chemical classes based on their

A

R groups

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8
Q

What is responsible for linking amino acids together to form polypeptides?

A

Dehydration synthesis

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9
Q

Two _______ joined together by a peptide bond form a dipeptide.

A

amino acids

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10
Q

Where are the peptide bonds located in a polypeptide?

A

Between the amino group of one amino acid and the carboxyl group of another

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11
Q

Proteins that only have a single polypeptide chain what two terms are synonymous?

A

Protein and polypeptide

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12
Q

Each kind of protein has a single unique sequence of

A

amino acids

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13
Q

In general, where are nonpolar and polar amino acid found in a folded protein?

A

Non-polar - interior

Polar - exterior

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14
Q

Type of interaction involves the formation of a covalent bond between two different amino acid side chains?

A

Disulfide bridge

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15
Q

The structure of proteins is usually discussed in terms of a hierarchy of how many levels?

A

4

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16
Q

The amino acid sequence of its polypeptides is

A

primary structures

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17
Q

Altering the sequence of amino acids in a polypeptide chain by just a single amino acid can have drastic effects on which of the following ?

A

Proteins function and proteins shape

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18
Q

What is true about the relationship between enzymes and environmental conditions?

A
  • the optimum conditions for enzyme activity are usually similar to the conditions where the enzyme normally functions
  • changing environmental conditions may alter the structure of enzymes
  • changing environment conditions may alter the activity of enzymes
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19
Q

Best describes the relationship between temp. and enzyme activity?

A

Each enzyme has an optimum temp. where it functions best

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20
Q

Proteins are made up of one or more unbranched chains of

A

amino acids

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21
Q

Denaturation

A

changes in a proteins environment cause the protein to unfold and lose its shape

22
Q

Primary structure

A

Amino acid sequence

23
Q

Secondary structure

A

Hydrogen bonding patterns. Alpha helices and Beta sheets

24
Q

Tertiary structure

A

folds and links. 3D folding of a single peptide

25
Q

Quaternary structure

A

interaction between 2 or more polypeptides to form a protein

26
Q

A protein’s _____ structure refers to the final 3 dimensional shape of the polypeptide chains make up the protein.

A

tertiary

27
Q

Interactions that help determine a protein’s tertiary structure

A
  • Hydrogen bonds
  • Disulfide bonds
  • Ionic bonds
  • Hydrophobic exclusion
28
Q

When a protein spontaneously refolds back into its natural environment it is called :

A

renaturation

29
Q

Protein denaturation may be caused by an increase in which of the following?

A
  • Temperature
  • Ionic concentration
  • pH
30
Q

Dissociation

A

observed when individual subunits making up a protein with quaternary structure separate without losing their tertiary structures

31
Q

Dehydration synthesis

A

responsible for linking amino acids together to form polypeptides

32
Q

The term ______ refers to a single, long chain of amino aicds, while a(n) _____ can be composed of one or more long amino acid chains.

A

polypeptide, protein

33
Q

In general, where are nonpolar and polar amino acids found in a folded protein?

A

Non- Polar - interior

Polar - exterior

34
Q

Hydrogen bonds between the amino and carboxyl groups of the polypeptide backbone help determine a proteins ____ structure while hydrogen bonds between the amino acid chains help determine protein _____ structure

A

secondary, tertiary

35
Q

TRUE OR FALSE

A protein’s final structure can include either regions shaped like an alpha helix or regions shaped like a B- pleated sheet but not both?

A

FALSE

36
Q

What are two basic types of secondary structure in proteins?

A

Alpha helix and B pleated sheet

37
Q

Individual polypeptides within a protein are referred to as which of the following?

A

subunits

38
Q

Most likely to be found in the interior of a protein:

A

Valine, Leucine, Phenylanine

39
Q

The alpha helix and b pleaded sheets are maintained primarily by hydrogen bonds between which of the following?

A

The amino and carboxyl groups within the polypeptide backbone

40
Q

A ____ is a substance or a mixture of substance’s pH

A

buffer

41
Q

A substance that decreases (H+) and increases pH when it dissociates in water is called

A

base

42
Q

A substance that increases (H+) and decreases pH when it dissociates in water is

A

acid

43
Q

Disulfide bridge

A

formation of a covalent bond between 2 cysteine side chains

44
Q

Ionic bond

A

formation of a bond between groups with opposite charge

45
Q

Van der Waals attraction

A

weak attraction between atoms due to oppositely polarized electron clouds

46
Q

Hydrophobic exclusion

A

hydrophobic portions of the protein gather in the interior of the protein

47
Q

Diffusion that is assisted by a channel protein or carrier protein is called ___ diffusion

A

facilitated

48
Q

channel proteins

A

have a hydrophilic interior that provides an aqueous channel through which polar molecules can pass when the channel is open

49
Q

TRUE about ions

A
  • They interact well with polar molecules

- They are repelled by the hydrophobic interior of the lipid bilayer

50
Q

Channel proteins that can be opened or closed in response to specific stimilus are called ____ channels

A

gated