Brainscape's Knowledge GenomeTM

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


See full index

Mbb 231 > Midterm 1 > Flashcards

Midterm 1 Flashcards

1
Q

Cell

A

The basic microscopic unit of all living beings; cell produces energy and uses it to build all the substances necessary for its life.

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

Organ

A

a fully differentiated structural and functional unit in an animal that is specialized for some particular function

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

The Nine properties of Cells

A

1.Cells are highly complex and organized
2.Have and express genetic code
3.Cells can reproduce
4.Cells acquire and utilize energy
5.Cells carry out a variety of chemical reactions
6.Cells engage in mechanical activities
7.Cells are able to respond to stimuli
8.Cells are capable of self-regulation
9.Cells evolve

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

catabolism

A

the break down of complex molecules

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

anabolism

A

set of metabolic pathways that construct molecules from smaller units.

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

Metabolism

A

sum total of chemical reactions in cells

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

How do cells transport materials around the cell

A

Motor proteins like actin fillaments or kinesin protein

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

Commonalities from eukaryotes and prokaryotes

A

1.an identical genetic language
2.a common set of metabolic pathways
3.many common structural features

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

Scale of a cell

A

10^-6 to 10^-9

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

What limits cell size

A

1)Surface area to volume ratio
2)Rate of diffusion
3)Sufficient space to perform reactions

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

Diffusion

A

unassisted motion that relies on concentration gradient

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Active transport

A

specialized machinery can move molecules/vesicles along the cytoskeleton from one place to another

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Requirements to be a model organisim

A

1)Relatively simple organisms
2)Fast generation time
3)Large numbers of offspring
4)Easy to manipulate in the lab
5)Inexpensive to breed

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

Hypothesis

A

statement consistent with most of the data, may take the form of a model (an explanation that appears to account for the data); must be testable

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Theory

A

a hypothesis that has been extensively tested by many investigators, using different approaches, widely accepted

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Law

A

a theory that has been tested and confirmed over a long period of time with virtually no doubt of its validity

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Virus

A

An infectious agent that can only replicate inside of a living cell.

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

Provirus

A

A virus genome that has been incorporated into the genome of its host.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

Virion

A

A complete viral particle, which includes the genome, capsid and in some cases an envelope

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

Viriod

A

An infectious agent that is composed solely of RNA (i.e., no coat proteins)

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

Prion

A

A infectious protein that can transmit its folded shape to other native folded proteins.

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

3 requirements of viral RNA

A

*for replication
*for packaging and delivery
*for modification of host cell

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

3 tenants of cell theory

A

1.All organisms are composed or one or more cells
2.The cell is the structural unit of life
3.Cells can arise only by division from a pre-existing cell

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

Hydrogen bonds

A

Weak attractive interaction between an electronegative atom and a hydrogen atom that is covalently linked to a second electronegative atom

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

Hydrophobic effects

A

Not a bond or attraction. These interactions are based on the desire of hydrophobic molecule to not interact with water.

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

Van der Waals Forces

A

Weak attractive forces between uncharged molecules that are very close to each other.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

4 main elements of life

A

H,N,O,C

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

The four types of macromolecules

A

1)Proteins
2)Nucleic Acids
3)Lipids
4)Carbohydrates

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
29
Q

Main functions of carbohydrates

A

1)Energy
2)Structural component of cell walls
3)Structural components of DNA and RNA
4)Used in protein signalling glycoprotiens

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
30
Q

General Formula of a carbohydrate

A

Cn(H2O)n

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

Ketose

A

monosaccharide containing one ketone group per molecule.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
32
Q

Aldose

A

a monosaccharide (a simple sugar) with a carbon backbone chain with a carbonyl group on the endmost carbon atom, making it an aldehyde, and hydroxyl groups connected to all the other carbon atoms.

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

Requirements for carbohydrate formation

A

Carbon chain of 5 or longer

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
34
Q

Anomeric carbon

A

the carbon derived from the carbonyl carbon (the ketone or aldehyde functional group) of the open-chain form of the carbohydrate molecule and is a stereocenter

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

Alpha bond

A

formed when both carbons have the same stereochemistry

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

α‐pyranose

A

when the OH group of the first carbon projects below the plane of the ring

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

β‐pyranose

A

when the hydroxyl OH of the first carbon projects upward from the plane of the ring

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

Beta Bond

A

formed by covalent bonding between the oxygen of the C1 (Carbon number 1) of one glucose ring and the C4 (carbon number 4) of the other connecting ring. The beta-1,4-glycosidic bond has the hydroxyl group pointing up.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
39
Q

Polysaccharides

A

Long chains of polymers of sugar and sugar derivitice that do not store information

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
40
Q

Main functions of poly saccharides

A

1)Storage or energy in glycogen and starch
2)Structural support in cellulose
3)Signalling using oligosaccharides

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
41
Q

Starch

A

Storage of energy in plants that form less organized chains with two different carbohydrates Amylose and Amylose pectin

42
Q

Glycogen

A

Storage of energy in animals, they are a monomer that forms highly complex long branches capable of forming coils

43
Q

Different types of structural polysaccarides

A

1)Cellulose
2)chitin
3)GAGS which fill inter cellular space

44
Q

How does alpha bond vs Beta bond affect structure

A

Alpha bonds are capable of forming coils where beta bonds form rigid rods

45
Q

Glycomics

A

systematic characterization of all of the carbohydrate components of a cell or tissue
(including those attached to proteins or lipids)

46
Q

O-linked

A

oligosaccharide in a glycosidic bond with a serine or threonine hydroxyl

47
Q

N-linked

A

oligosaccharide in a glycosidic bond to the amide nitrogen of an Asparagine residue

48
Q

Nucleic acid composition

A

1)5 carbon sugar
2)Phosphate group
3)N-containing aromatic bases

49
Q

Purines

A

Guanine and Adenine

50
Q

Pyrimidines

A

Cytosine,Thymine,Uracil

51
Q

Difference between G-C and A-T bonds

A

G-c forms 3 bonds where as A-T forms only 2 bonds

52
Q

Which way is dna built?

A

5’ to 3’

53
Q

Different types of noncoding RNA

A

snRNA-Regulate molecules
MiRNA-Regulate gene expression
tRNA-Builds protiens
rRNA-Scaffodling for ribosomes
incRNA-Act as protiens

54
Q

Six types of Lipids

A

1)Fatty acid, Saturated or Unsaturated
2)Triglycerols
3)Phospholipids
4)Steroids
5)Glycolipids
6)Terpenes

55
Q

What is this

A

Fatty acid

56
Q

Saturated vs unsaturated Fatty acid

A

saturated fatty acids have no double bonds are are straight chains of CH bonds where as unsaturated has a double bond causing a kink in the chain

57
Q

Fatty Acid

A

a long unbranched hydrocarbon chain with a carboxyl group at one end they influence cell and tissue metabolism, function, and responsiveness to hormonal and other signals

58
Q

Trans fat vs Cis Fat

A

Normal fatty acid is in the cis conformation where both ends of the double bond are on the same side where as trans fats have the substituent on either side of the double bond

59
Q

Hydrogenation

A

a chemical process by which hydrogens are added to mono-unsaturated or poly-unsaturated fats to reduce the number of double bonds

60
Q

Why do unsaturated stick together better than saturated ones

A

Unstaurated fats have a kink in them at their double bonds reducing van der whal interactions

61
Q

Triacylglycerols

A

also known as triglycerides, consist of a glycerol molecule with three fatty acids attached to it

62
Q

What is this

A

Triacylgerols

63
Q

Glycerol

A

a three-carbon alcohol with a hydroxyl group on each carbon

64
Q

Tail portion of a triacylglycerol

A

Fatty acids are linked to glycerol, one at a time, by esterbonds formed by the removal of water

65
Q

Function of Triaclglycerols

A

Energy storage and insulation of the body

66
Q

Phospholipids

A

they have two ends with different properties: one end contains a phosphate group (hydrophilic); the other end has fatty acid tails (hydrophobic

67
Q

What is this

A

Phospholipid

68
Q

Describe the anatomy of a phospholipid

A

A phospholipid molecule has two fatty acid chains attached to a glycerol backbone = diacylglycerol and The third hydroxyl of glycerol is bonded to a phosphate group, which is bonded to a small polar group like choline.

69
Q

Steroids

A

are derivatives of a four-ringed hydrocarbon skeleton that act as signalling throughout the body

70
Q

Terpenes

A

are synthesized from the five-carbon compound isoprene and are sometimes called isoprenoids important mediators of ecological interactions. For example, they play a role in plant defense against herbivory, disease resistance, attraction of mutualists such as pollinators, as well as potentially plant-plant communication.

71
Q

What is MW or molecular weight for amino acids and proteins measure in

A

Dalton, one twelfth the mass of Carbon-12

72
Q

What are all amino acids composed of

A

1.carboxyl group
2.amino group
3.single carbon atom,the α‐carbon
4. unique side chain,called an R group

73
Q

Which way is a protein synthesized

A

N terminus to C terminus

74
Q

Purpose of charged amino acids

A

Capable of forming ionic bonds

75
Q

Purpose of polar amino acids

A

Found on the surfaces of proteins and are involved in H bonding

76
Q

Purpose of Non-polar amino acids

A

Buried inside the core of proteins and allow for hydrophobic interactions and vanderwhal interactions

77
Q

Conformation vs Configuration

A

Conformation is the 3-d shape a protein will assume when folded where as configuration is what the molecular composition of a protein is

78
Q

Primary structure

A

Amino acid residues within a protein

79
Q

Secondary structure

A

Alpha helices, Beta sheets, turns and loops that are generated from the interactions between the poly peptide backbone (CO and NH groups)

80
Q

Number of amino acids per alpha helix turn

A

3.6

81
Q

Alpha Helix constrains

A

1.Electrostatic repulsion (or attraction) between successive amino acid residues with charged R groups
2.Bulkiness of adjacent R groups
3.Interactions between R groups spaced three (or four) residues apart
4.“Helix forming” amino acids include: Leucine (L), Methionine (M), Glutamate (E)
5.“Helix breakers” include Proline (P) and Glycine (G) residues

82
Q

Beta sheet forming amino acids

A

Isoleucine (I), Valine (V) and Phenylalanine (F)

83
Q

What does this depict

A

Anti-parallel beta sheets

84
Q

What does this depict

A

Parallel Beta sheets

85
Q

Motifs

A

Certain combinations of secondary structures are common among many different proteins Structural motifs often perform common functions in different proteins

86
Q

Tertiary structure

A

3-D shape of a protein stabilized by covalent and noncovalent bonds between the side chains of the protein

87
Q

X‐ray crystallography

A

Provides higher resolution structures for larger proteins, but is limited by the ability to get any given protein to form pure crystals

88
Q

Nuclear magnetic resonance (NMR) spectroscopy

A

provides information about dynamic changes in structure, and can rapidly reveal drug binding sites, but is difficult to use on larger proteins

89
Q

Interactions that hold a tertiary structure together

A

1.Hydrogen Bonds
2.Ionic Bonds
3.Van Der Waals Interactions
4.Hydrophobic Interactions
5.Disulfide Bridges (between Cysteine residues)

90
Q

Domain

A

is a discrete locally folded unit (i.e., as substructure) of the overall tertiary structure, usually with a specific function

91
Q

Homodimer

A

a protein composed of two identical subunits

92
Q

Heterodimer

A

a protein composed of two non-identical subunits

93
Q

Monomeric

A

Proteins that consist of a single polypeptide

94
Q

multimeric proteins

A

consist of two or more polypeptides

95
Q

native conformation

A

stable three-dimensional structure for a particular polypeptide

96
Q

Fibrous Proteins

A

Have extensive regions of secondary structure, giving them a highly ordered, repetitive structure, these are typically found outside of the cell like hair,keratin,collegen

97
Q

Globular Proteins

A

Different segments of a polypeptide chain (or multiple polypeptide chains) fold back on each other generating a compact structure.Each type has its own unique tertiary structure, which provides structural diversity necessary for proteins to carry out a wide array of biological functions

98
Q

Self Assembly

A

The primary sequence of amino acids contained all of the information required for the formation of the polypeptide’s 3D conformation

99
Q

How do proteins determine their native state?

A

They likely explore a range of conformations, then funnel down to the most energetically favourable state.

100
Q

Molecular chaperone

A

bind to short stretches of hydrophobic amino acids that are exposed in non-native proteins to facilitate proper folding

101
Q

How do prions damage the body

A

Prions are misfolded protiens that when in contact with other native proteins causes them to reconfigure into a prion. These prions aggregate forming plaques in the body

102
Q
A

Mbb 231 (5 decks)

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