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Bio 116H Dr Balish/Zhao > Exam 1(pre ME 1) > Flashcards

Exam 1(pre ME 1) Flashcards

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Biology 101 flashcards
1
Q

How do electrons lose/gain energy?

A

They gain energy by moving away from the nucleus or to higher energy levels and lose energy by moving toward the nucleus or to lower energy levels

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2
Q

Covalent bond

A

Chains and functional groups, hardest to break(strongest) in aqueous(living) environments

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3
Q

Ionic bonds

A

Holds something together until something with a stronger affinity pull it apart

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4
Q

Hydrogen bonds

A

Weakest bonds in aqueous environments, but strong in larger numbers

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5
Q

Which interactions does signaling involve and why

A

Ionic and hydrogen bonds because covalent bonds are hardest to break/pass stuff on with

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6
Q

What attracts H20 and NH3+ ?

A

The slight positive charge in the Hydrogen in water attracts to the slight negative charge in the N in ammonia

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7
Q

In what case can H bonds disrupt ionic bonds?

A

They can disrupt ionic bonds when the higher number of H bonds making the total force of H bonds stronger than the total force of ionic bonds

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8
Q

What is the type of bond between H and O in H2O?

A

Polar covalent bonds(sharing electrons)

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9
Q

Properties of polar substances

A

Hydrophilic, can dissolve in water, electrons not shared equally, lots of branching

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10
Q

Properties of nonpolar substances

A

Hydrophobic, can not dissolve in water, planar/flat, little branching

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11
Q

Amphipathic+example

A

A substance with polar and nonpolar components

example: DNA

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12
Q

What allows earth to have liquid oceans?

A

Solid water is less dense than liquid water so it floats, keep the oceans from freezing

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13
Q

Which properties of water make it critical to life?

A
  1. Surface tension
  2. Cohesion/adhesion
  3. Support
  4. Dehydration/hydrolysis
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14
Q

Which part of the plants moves water up?

A

xylem

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15
Q

What allows the xylem to move water up a plant

A

cohesion/adhesion

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16
Q

How can water provide support?

A

Through pressure mechanisms like hydrostatic skeletons

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17
Q

What role do dehydration and hydrolysis reactions play

A

Dehydration reactions build macromolecules(make covalent bonds), hydrolysis breaks them down(break covalent bonds)

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18
Q

Example of hydrolysis

A

cellular respiration

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19
Q

What role does pH play in macromolecules of living things

A

pH affects structure, therefore affecting function. cells often manipulate function by changing pH

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20
Q

What makes carbon special?

A

It has 4 bonding sites and can bond to many different kinds of atoms

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21
Q

Hydroxyl groups

A

-OH

Essential in formation of DNA, RNA and proteins, very reactive

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22
Q

Carboxyl groups

A

-COOH

Essential in protein formation

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23
Q

Phosphate

A

-OPO3(2-)

Important in the structure of DNA/RNA

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24
Q

How do you change the function of molecules?

A

alter its shape/structure

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25
Q

Variety of proteins compared to DNA/RNA and why

A

proteins have more variety because they have more building blocks

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26
Q

Big four atoms and the next 2 most common atoms

A

big four: C, N, O and H

next 2 most common: P and S

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27
Q

What are carbohydrates made of?

A

C, H and O

compounds of C and H2O

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28
Q

What molecules do carbohydrates form?

A

Monosaccharides, dissacharides and polysaccharides

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29
Q

Glucose in aqueous environments

A

Will usually circularize

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30
Q

Monosaccharides

A

Have different numbers of carbons, simple sugars, ring or linear, glucose, ribose, deoxyribose

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31
Q

How many carbons are in the building blocks of DNA/RNA?

A

5

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32
Q

What sugar does DNA have and what makes it important

A

deoxyribose, it is missing a hydroxyl group

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33
Q

Why is glucose a preferred energy source for cells?

A

It is easier to break down

34
Q

Glycosidic linkage

A

Covalent bond that our bodies metabolize easily

35
Q

Dissacharides

A

2 monosaccharides, sucrose, lactose, maltose

36
Q

Polysaccharides

A

have many different function, long term energy storage, glycogen, starch, cellulose, chitin, peptidoglycan

37
Q

Starch

A

Polysaccharide used by plants for long term energy storage, monomers of glucose put together, low solubility, branching

38
Q

Lipids

A
  • nonpolar/hydrophobic
  • long term energy storage
  • fats, triglycerides, steroids and hormones
39
Q

Carbon to carbon bond characteristics

A

Flat, planar, nonpolar, lacking O

40
Q

Saturated vs Unsaturated fatty acids

A

Saturated: Carbon saturated with H, solid at room temp, can be packed together making it solid

Unsaturated: Kink/bend, more common in plants, carbon-carbon double bond, liquid at room temp, can not be packed together because of kinks making it liquid

41
Q

Phospholids

A
  • Amphipathic
  • Crucial to membrane structure
  • Circular polar heads, lobe shaped fatty acid tails
42
Q

Glycerol backbone

A

3 carbon backbone: 2 hydrophobic, nonpolar fatty acids attached to 1 polar, hydrophilic phosphate head(amphipathic)

43
Q

Steroids

A
  • 4 fused rings
  • critical signaling molecules
  • control gene activities
  • Nonpolar, planar
  • Can interact with DNA by going into the cell nucleus to turn off genes
  • Can diffuse across membranes
44
Q

What are proteins known as?

A

The workhorse of the cell

45
Q

What do proteins contain

A
  • Big four elements(C, H, O, N)
  • Some contain S in essential amino acids
  • 20+ amino acid building blocks
46
Q

Essential amino acids

A

amino not acids not made by the body that must be retrieved

47
Q

Enzymes

A
  • most are proteins

* end in -ase

48
Q

Amino acid structure

A

Carbon bonded to an amino group, a carboxyl group, H, and a side chain R group

49
Q

Sources of diversity in amino acids/proteins

A
  • Different R groups in every acid

* more than 20 amino acid building blocks

50
Q

What role does polarity play in protein structure?

A

Nonpolar groups end up pointing inside of the protein as it folds, polar groups point outside

51
Q

Peptide bonds

A
  • How amino acids connect
  • C and N on the end of amino acids hook together to form chains which or called peptide bonds
  • formed through dehydration synthesis
52
Q

Polypeptide

A
  • linear chain of 4 or more amino acids

* Amino acids makeup the front end, a carboxyl group makes up the back end

53
Q

Primary structure

A
  • 1st hierarchal level of protein structure
  • determine by gene sequence
  • Order of amino acids
54
Q

Secondary structure

A
  • 2nd hierarchal level of protein structure
  • Repeating patterns that are determined by chemical and physical properties of amino acids(primary structure)
  • made of of alpha spiral helixes and folded beta pleated sheats held in place by hydrogen bonds
  • refers local interaction if R groups
  • Affects atoms that are close to each other
55
Q

Tertiary structure

A

•3rd hierarchal level of protein structure
•Complex 3D shapes
Proteins fold back and forth on themselves
•Allows portions of protein at long distances to interact

56
Q

Quaternary structure

A
  • 4th hierarchal level of protein structure
  • Interactions of multiple polypeptides
  • Note all proteins have this level of structure
57
Q

5 factors promoting protein folding and stability

A
  1. H bonds
  2. Ionic bonds
  3. Hydrophobic effects
  4. Van der Waals forces (attractive forces)
  5. Disulfide bridges
58
Q

Disulfide bridges

A

Covalent bonds between 2 sulfurs and R groups

59
Q

How are DNA/RNA related to nucleic acid?

A

they are polymers of nucleic acid

60
Q

Building blocks of DNA and RNA

A

Both: 5 carbon sugar attached to a sugar-phosphate backbone group and nitrogenous base

DNA bases: GATC
RNA bases: GUAC

61
Q

DNA and RNA function

A

DNA: Store genetic info

RNA: critical in info expressions, has many types, can do work, functions are still being learned about

62
Q

What holds nucleic acids together?

A

H bonds

63
Q

Nucleic acid structure, which type of molecule do they structurally resemble?

A

Planar, flat, stacked, nonpolar, like steroids

64
Q

DNA structure

A
  • Antiparallel 5’ and 3’ ends that are complementary to base pairs
  • has long ribbons of covalent linkages between sugar and phosphate
  • Inside is stable, outer part has lots of negatively charged phosphates
65
Q

RNA structure

A
  • Single stranded
  • 5’ and 3’ ends
  • can be 3D and complex
  • complementary to nucleic acids
  • secondary structure
  • has a ribbon like, negatively charged sugar phosphatebackbone
66
Q

How does diversity of nucleic acids and proteins compare

A

Nucleic acids can be diverse but not like proteins

67
Q

Effects of cholesterol on membrane

A

In warm temps: cholesterol stabilizes the membrane and makes it less fluid

In cold temps: makes membranes more fluid, acts as antifreeze

Present in all cell membranes

68
Q

What does fluidity of the membrane depend on?

A
  1. Length of FA chains: Shorter FA chains=more fluid and vice versa
  2. Degree of saturation: More saturated=less fluid
  3. Cholesterol
69
Q

What do all cells have?

A
  1. Cell membrane
  2. Cytoplasm/cytosol
  3. Ribosomes
  4. DNA-based genome
  5. ATP for energy
70
Q

Ribosomes

A

make proteins and replenish proteins who have fallen into disrepair

71
Q

Glycoprotein

A

Proteins in cell membrane that has polar sugars attached to it with positive and negative charges(water friendly) to keep the cell hydrated. Recognizes other cells

72
Q

Endoplasmic reticulum

A

(ER) Conducts protein synthesis

Split into rough and smooth ER
Rough: protein synthesis
Smooth: lipid synthesis

73
Q

Golgi

A

Packing and transport within cell, stacks of membrane

74
Q

Endomembrane system

A

present ONLY in eukaryotes, used to move stuff around

75
Q

Molecules with high, moderate, low and very low permeabilities

A

High: Gases, small and uncharged polar molecules

Moderate: Water, urea

Low: Organic polar molecules

Very low: ions, charged polar molecules, macromolecules

76
Q

Hypotonic vs hypertonic

A

Hypotonic: less concentrated

Hypertonic: more concentrated

77
Q

Membrane protein functions

A
  1. transport
  2. enzymatic activity
  3. Signal transduction
  4. Cell-cell recognition
  5. intercellular joining
  6. Attachment to cytoskeleton and extracellular matrix
78
Q

nucleolus

A

inside nucleus, transcribed and assembles ribsomes

79
Q

Which part of the ER is close to the nucleus?

A

Rough ER

80
Q

Atoms that make up carbs, lipids and proteins

A

Carbs: C, H, or O

Proteins: C, H, O, N

Lipids: C, H, O

Bio 116H Dr Balish/Zhao (6 decks)

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