Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

Human physiology > Chapter 2: Molecular Interactions > Flashcards

Chapter 2: Molecular Interactions Flashcards

1
Q

What are the four major groups of macromolecules?

A

carbohydrates
lipids
proteins
nucleotides

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

what can macromolecules combine to form?

A

glycoproteins, glycolipids, lipoproteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

*are biomolecules made mostly of carbon and hydrogen
*lipids have a backbone of
glycerol and 1–3 fatty acids
*are nonpolar and
therefore not very soluble in water

A

lipids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

what are the two categories of lipids?

A

fats

oils

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q 
are long chains of carbon atoms bound to hydrogens, with
a carboxyl (–COOH) or “acid” group at one end of the chain
A

fatty acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

*have no double bonds between carbons, so they
are “saturated” with hydrogens

*solid at room temp

A

saturated fatty acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

*have one double bond between two of
the carbons in the chain
*For each double bond, the molecule has two
fewer hydrogen atoms attached to the carbon chain

A

monounsaturated fatty acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

have two or more double bonds

between carbons in the chain.

A

polyunsaturated fatty acid

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

what are 3 types of lipid related molecules?

A

eicosanoids
steroids
phsopholipids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

modified 20-carbon fatty acids with a
complete or partial carbon ring at one
end and two long carbon chain “tails.”

A

eicosanoids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

lipid-related molecules whose structure

includes four linked carbon rings

A

steroids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q
  • *have 2 fatty acids and a phosphate group (–H2PO4)

* *important component of cell membrane

A

phospholipids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q
  • the most abundant biomolecule

* that for each carbon there are two hydrogens and one oxygen

A

carbohydrates

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

what are the 3 categories of carbohydrates?

A

monosaccharides
disaccharides
polysaccharides

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q
  • simple sugars
  • building blocks of complex carbohydratess
  • examples are ribose and glucose
A

monosaccharides

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q
  • consist of glucose plus another monosaccharide

* examples are sucrose, maltose, lactose

A

disaccharides

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q
  • glucose polymers
  • glucose is stored in this form for energy
  • animals (chitin & glycogen)
  • plants (cellulose & starch)
  • yeast/bacteria (dextran)
A

polysaccharide

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

polymers of smaller building block molecules called amino acids

A

proteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q
  • have a carboxyl group (–COOH), an amino group (–NH2), and a hydrogen attached to the same carbon
  • The fourth bond of the carbon attaches to a variable “R” group
A

amino acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

bond in which the amino group of one amino acid joins the carboxyl group of the other, with the loss of water.

A

peptide bond

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

what are the different structures of proteins?

A

primary
secondary
tertiary
quaternary

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

*The sequence of amino acids in a peptide chain

A

primary structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q
  • Covalent bond angles between amino acids determine secondary structure
  • alpha helix or beta pleated sheets
A

secondary structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q
  • protein’s 3D shape
  • fibrous proteins (collagen)
  • globular proteins
A

tertiary structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q
  • Multiple subunits combine with noncovalent bonds

* Hemoglobin molecules are made from four globular protein subunits

A

quaternary structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

*biomolecules that play an important role in energy and information transfer

*consists of (1) one or more phosphate
groups, (2) a 5-carbon sugar, and (3) a carbon-nitrogen ring structure called a
nitrogenous base

A

nucleotide

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q
  • nucleotide polymers
  • RNA and DNA
  • store and transmit genetic information
A

nucleic acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
28
Q

include energy transferring compounds such as ATP, ADP, cyclic AMP

A

single nucleotides

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
29
Q
  • have a double ring structure
  • nitrogenous base
  • include adenine and guanine
A

purines

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
30
Q
  • have a single ring structure
  • nitrogenous base
  • includes cytosine, thymine, uracil
A

pyrimidines

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
31
Q

what are the 2 functions of single nucleotides?

A
  • capture and transfer energy in high energy electrons or phosphate bonds
  • aid in cell-cell communication
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
32
Q

what is the function of ATP, ADP, NAD, FAD?

A

energy capture and transfer

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
33
Q

what is the function of cAMP?

A

cell-cell communication

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
34
Q
  • smallest particle of any element
  • link by sharing electrons to form molecules
  • consist of protons, neutrons, and electrons
A

atom

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
35
Q

what are the three elements that make up 90% of our body mass?

A

oxygen
carbon
hydrogen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
36
Q

simplest type of matter

A

elements

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
37
Q

determine the element (atomic #)

A

protons

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
38
Q

determine the isotope

A

neutrons

39
Q
  • form covalent bonds
  • create ions when gained or lost
  • capture and store energy
  • create free radicals
A

electrons

40
Q

an atom that gains or loses neutrons becomes….

A

an isotope of the same element

41
Q

an atom that gains or loses electrons becomes an…..

A

ion of the same elements

42
Q

lipids + proteins

A

lipoproteins

43
Q

proteins + carbohydrates

A

glycoproteins

44
Q

carbohydrates + lipids

A

glycolipids

45
Q

the units formed when two or more atoms link by sharing electrons

A

molecules

46
Q

the links between atoms, which are formed by transferring/sharing of electrons

A

bonds

47
Q

what are the main two types of bonds?

A

covalent bonds

noncovalent bonds

48
Q
  • result when atoms share electrons
  • these bonds require the most energy to make or break
  • include nonpolar molecules and polar molecules
A

covalent bonds

49
Q
  • have an even distribution of electrons

* molecules made of mostly carbon and hydrogen are usually this

A

nonpolar molecules

50
Q
  • have regions of partial charge

* example is water

A

polar molecules

51
Q

includes ionic bonds, hydrogen bonds, and Van der Waals Forces

A

noncovalent bonds

52
Q
  • electrostatic attractions between ions

* example is NaCl

A

ionic bonds

53
Q
  • forms between a hydrogen atom and a nearby oxygen, nitrogen, or fluorine atom
  • responsible for surface tensions
A

hydrogen bonds

54
Q

weak, nonspecific attractions between atoms

A

Van der Waals Forces

55
Q 
*Molecules that have polar
regions or ionic bonds readily
interact with the polar regions
of water.
*This enables them to
dissolve easily in water
A

hydrophilic

56
Q
  • Water molecules interact with ions or other polar molecules to form hydration shells around the ions.
  • This disrupts the hydrogen bonding between water molecules, thereby lowering the freezing temperature of water
A

hydrophilic interactions

57
Q

have polar heads and nonpolar tails

A

phospholipid molecules

58
Q

**Because they have an even distribution of electrons and no positive or negative poles, nonpolar molecules have no regions of partial charge, and therefore tend to repel water molecules
**Molecules like
these do not dissolve readily
in water

A

hydrophobic interactions

59
Q

What are the categories of proteins?

A
  1. enzymes
  2. membrane transporters
  3. signal molecules
  4. receptors
  5. binding proteins
  6. immunoglobulins
  7. regulatory proteins
60
Q

biological catalysts

A

enzymes

61
Q

found in the ECF and transport molecules within the body

A

binding proteins

62
Q
  • antibodies

* help protect the body from foreign invaders

A

immunoglobulins

63
Q

turn cell processes on and off or up and down

A

regulatory proteins

64
Q

Any molecule or ion that binds to another molecule

A

ligand

65
Q

how can proteins bind to other molecules?

A

noncovalent interactions on binding sites

66
Q

model of protein binding where the binding site shape is not an exact match to the ligands’ (L) shape

A

Induced fit model of protein-ligand binding

67
Q

the degree to which a protein is attracted to a ligand

A

affinity

68
Q

are protein binding reactions reversible

A

yes

69
Q
  • states that when a reaction is at equilibrium, the ratio of the products to the substrates is always the same
  • binding reactions obey this law
A

law of mass action

70
Q

what does a higher affinity for a ligand mean?

A

a larger Keq

71
Q

equation of the equilibrium for a reaction

A

Keq= [PL]/[P][L]

72
Q

reciprocal of the equilibrium equation

A
  • is the dissociation constant

* Kd= [P][L]/[PL]

73
Q

what does a lower affinity for a ligand mean?

A

a larger Kd

74
Q

what happens during a reaction at equilibrium?

A

rate of reaction in forward direction (r1) = the rate of reaction in the reverse direction (r2)

75
Q

what is the ratio of bound to unbound at equilibrium?

A

it is always the same

76
Q
  • closely related proteins whose function is similar but whose affinity for ligand differs
  • alters protein binding
A

isoforms

77
Q

has increased affinity for oxygen

A

fetal isoform of hemoglobin

78
Q
  • alters protein binding

* synthesized in an inactive form and must become activated

A

activation protein

79
Q

how do the activation proteins become activated?

A
  • enzymes remove portions of the protein

* may require cofactors that must attach to the protein before the binding site becomes active

80
Q

how are inactive forms of proteins identified?

A

prefix pro- or suffix -ogen added to the name of the active enzyme

81
Q
  • protein is inactive until peptide fragments are removed

* essential for binding activity

A

proteolytic activation

82
Q
  • essential for binding activity

* required for ligand binding at the binding site

A

cofactors

83
Q
  • alters protein binding

* a factor that influences either protein binding or protein activity

A

modulation

84
Q

what are the 2 mechanisms of modulation?

A
  1. The modulator changes the proteins ability to bind the ligand
  2. The modulator changes the proteins ability to create a response.
85
Q

a modulator that binds to protein

away from binding site and turns it on

A

allosteric activator

86
Q

a modulator that binds to protein away

from binding site and inactivates the binding site

A

allosteric inhibitor

87
Q

blocks ligand binding at the binding site

A

competitive inhibitor

88
Q
  • alters proteins binding

* the programmed production of new proteins (enzymes, receptors, membrane transport proteins)

A

up-regulation

89
Q
  • alters protein binding

* the programmed removal of proteins

A

down-regulation

90
Q

How do temperature and pH affect proteins?

A
  • may disrupt protein structure and cause loss of function

* can be irreversible if the protein becomes denatured

91
Q

What happens if the protein concentration in the cell is constant?

A

the magnitude of the response is determined by the concentration of the ligand.

92
Q

what does increased ligands result in?

A

increase in response

93
Q

occurs when all the protein binding sites are occupied

A

saturation

Human physiology (17 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions