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Biology I > Ch.3 Carbon and the Molecular Diversity of life > Flashcards

Ch.3 Carbon and the Molecular Diversity of life Flashcards

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1
Q

A compund containing carbon is said to be?

A

Organic Compound

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2
Q

Critically important large molecules of all living things fall into four main classes, what are they?

A

Carbohydrates

Lipids

Proteins

Nucleic acids

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3
Q

Methane chemical formula

And Molecular shape

A

CH4

Tehrahedron

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4
Q

Ethane chemical formula

and

Molecular shape

A

C2H6

Two overlaping tetrahedrons

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5
Q

Ethene (ethylene)

Formula

And

Shape

A

C2H4

Two Carbon atoms are joined by double bond

All molecules attached to those carbons are in the same plane

THIS MOLECULE IS FLAT

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6
Q

What are the four main atoms in an organic molecule?

And

How many Valence electrons do they each have?

A
  1. Hydrogen Valence =1
  2. Oxygen Valence = 2
  3. Nitrogen Valence = 3
  4. Carbon Valence =4
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7
Q

The number of unpaired electrons in the valence shell of an atom generally equal the atoms what?

And what does that mean for the atoms bonding?

A

Valence

That is the number of bonds the atom can form

Ex, Hydrogen has one valence so it can form one bond.

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8
Q

Is a Carbon is bonded to four other atoms what Molecular shape does it make?

A

Tetrahedral Shape

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9
Q

What is a Hydrocarbon

A

Organic molecules consisting of only Carbon and Hydrogen.

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10
Q

Petroleum is made up of what?

A

Hydrocarbons

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11
Q

What do lipids and petroleum have in common and why arent they able to do this?

A

They are both Hydrophobic and it is because they are both non-polar

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12
Q

What are the four ways that carbon skeltons and vary?

A

Length

Branching

Double bond position

Presence of rings

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13
Q

Define an Isomer, and name the three types

A

Compounds that have the same number if atoms of the same elements, but different structures and hence different properties.

Structural isomers

Cis-trans isomers

and

Enantiomers

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14
Q

Structural isomers

A

Strutural isomers differ in the covalent arrangments of their atoms.

The number of possible isomers increases as carbon skeletons increase in size

Structual isomers also might differ in location of double bonds

Example,

C5H12

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15
Q

Cis-trans isomers

A

carbons have covalent bonds to the same atoms, but the atoms differ in their spatial arrangement due to inflexibility of double bonds

The subtle differences in shape between such isomers can greatly affect the activities of organic molecules

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16
Q

Enantiomers

A

are isomers that are mirror images of one another and differ in shape due to the presence of an asymmetric carbon

Enantiomers are left-handed and right-handed versions of the same molecule

Usually only one isomer is biologically active

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17
Q

What are the names of the 7 functional groups and what do they do?

A

Chemical groups can replace one or more of the hydrogens bonded to the carbon skeleton of a hydrocarbon

Functional groups are the chemical groups that affect molecular function by being directly involved in chemical reactions

Each functional group participates in chemical reactions in a characteristic way

The seven functional groups that are most important in the chemistry of life:

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  1. Hydroxyl group
  2. Carbonyl group
  3. Carboxyl group
  4. Amino group
  5. Sulfhydryl group
  6. Phosphate group
  7. Methyl group
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18
Q

Adenosine Triphosphate (ATP)

A

An organic phosphate molecule, adenosine triphosphate (ATP), has an important function in the cell

ATP consists of an organic molecule called adenosine attached to a string of three phosphate groups

ATP stores the potential to react with water, releasing energy that can be used by the cell

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19
Q

Macromolecules

A

a molecule containing a very large number of atoms, such as a Carbohydrates, protein, nucleic acid, or synthetic polymer.

Macro (LARGE)

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20
Q

Polymer

A

is a long molecule consisting of many similiar or identical building blocks linked by covalent bonds.

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21
Q

Monomers

A

(Greek for mono meaning single)

The repeating units that serve as the building blocks of a polymer.

Some molecules that serve as monomers also have other functions of their own

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22
Q

Enzymes

A

Specialized macromolecules (usually proteins) that speed up chemical reactions.

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23
Q

Dehydration Reaction

A

occurs when two monomers bond together through the loss of a water molecule

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24
Q

Hydrolysis

A

A process that is essentially the reverse of the dehydration reaction.

Hydrolysis means water breakage

(from Greek Hydro, water and Lysis, break)

The bond between monomers is broken by the addition of a water molecule, with a hydrogen from water attaching to one monomer and the hydroxyl group attaching to an another.

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25
Q

Carbohydrates

A

Include both sugar and polymers of sugar.

The simplest carbohydrates are the monosaccharides, or simple sugars. These are the monomers from which more complex carbohydrates are built.

Disaccharides are double sugars, consisting of two monosaccharides joined by a covalent bond.

Carbohydrates also include macromolecules called polysaccharides, polymers composed of many sugar building blocks joined together by dehydration reaction.

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26
Q

Monosaccharides

A

(from the Greek monos, single, and sacchar, sugar)

Monosaccharides have molecular formulas that
are usually multiples of CH2O

Glucose (C6H12O6) is the most common

monosaccharide

Monosaccharides are classified by the number of
carbons in the carbon skeleton and the placement
of the carbonyl group.

The Carbon skeleton of a sugar molecule ranges from 3-7 carbons long!

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27
Q

Ketone

A

when the carbonyl group is within the carbon skeleton.

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28
Q

Aldehyde

A

If the carbonyl group (>C=O) is at the end of a carbon skeleton

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29
Q

What is the difference between a fructose and glucose carbon skeleton?

A

Glucose and fructose are both hexoses C6H12O6 (containing 6 carbon atoms) in their skeleton

The differenc is glucose is a aldehyde (containg the carbonyl outside the skeleton)

and

Fructose is a Ketone (carbonyl inside the carbons skeleton)

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30
Q

What shape do sugars make when in aqueous solutions

A

Though often drawn as linear skeletons, in aqueous solutions many sugars form rings

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31
Q

Disaccharide

A

Two monosacharides joined together by (glycosidic linkage), a covalent bond formed between two monosaccharides by a dehydration reaction.

32
Q

glycosidic linkage

A

(glyco = carbohydrates)

a covalent bond formed between two monosaccharides by a dehydration reaction.

33
Q

Polysaccharides

A

the polymers of sugars, have storage and structural roles

The structure and function of a polysaccharide are determined by its sugar monomers and the positions of glycosidic linkages

34
Q

Starch

A

a storage polysaccharide of plants, consists entirely of glucose monomers

§Plants store surplus starch as granules

Most animals have enzymes that can hydrolyze plant start, making glucose available as a nutrient

35
Q

Glycogen

A

is a storage polysaccharide in animals

Humans and other vertebrates store glycogen mainly in liver and muscle cells

36
Q

Cellulose

A

The polysaccharide cellulose is a major component of the tough wall of plant cells

Like starch and glycogen, cellulose is a polymer of glucose, but the glycosidic linkages in cellulose differ

The difference is based on two ring forms for glucose

37
Q

Enzymes that digest starch by hydrolyzing “a” linkages can’t hydrolyze “b” linkages in cellulose.

What happeneds to the the b linkages of cellulose the system

Give some examples of cellulose

A

Cellulose in human food passes through the digestive tract as insoluble fiber.

Some microbes use enzymes to digest cellulose

Many herbivores, from cows to termites, have symbiotic relationships with these microbes

38
Q

How do the molecules of glycosidic linkages in starch and celluslose differ?

A

Certain starch molecules are largely helical.

the cellulose molecule is straight

39
Q

What is chitin?

A

another structural polysaccharide (polymers with a few hundred to few thousand glycosidic linkages), is found in the exoskeleton of arthropods

Chitin also provides structural support for the cell walls of many fungi

40
Q

Lipids

A

do not form true polymers

The unifying feature of lipids is having little or no affinity for water

Lipids are hydrophobic because they consist mostly
of hydrocarbons, which form nonpolar covalent bonds

The most biologically important lipids are

  • fats,
  • phospholipids, and
  • steroids
41
Q

Fats are constructed from two types of smaller molecules:

Name them

A

glycerol and fatty acids

Glycerol is a three-carbon alcohol with a hydroxyl group attached to each carbon

42
Q

A fatty acid consists of What?

A

A fatty acid consists of a carboxyl group attached to a long carbon skeleton

43
Q

Saturated fatty acids

A

have the maximum number of hydrogen atoms possible and no double bonds

44
Q

Unsaturated fatty acids

name two types

A

Unsaturated fatty acids have one or more double bonds

Plant fats and fish fats are usually unsaturated

45
Q

Which type of fat do animals mainly consist of?

A

Fats made from saturated fatty acids are called saturated fats and are solid at room temperature

Most animal fats are saturated

46
Q

phospholipid

A

two fatty acids and a phosphate group are attached to glycerol

The two fatty acid tails are hydrophobic, but the phosphate group and its attachments form a hydrophilic head

Phospholipids are major constituents of cell membranes

47
Q

Steroids

A

are lipids characterized by a carbon skeleton consisting of four fused rings

48
Q

Cholesterol

A

Cholesterol, an important steroid, is a component in animal cell membranes

Although cholesterol is essential in animals, high levels in the blood may contribute to atherosclerosis

49
Q

Ezymatic proteins

A

Function:

Selective acceleration of chemical reactions

ex

Disgestive enzymes catalyze the hydrolysis of bonds in food molecules.

50
Q

Defensive proteins

A

Function:

Protection against disease

Example,

Antibodies inactivate and help destory viruses and bacteria.

51
Q

Storage proteins

A

Functions:

Storage of amino acids

52
Q

transport proteins

A

Function:

Transport of substances

53
Q

Hormonal proteins

A

Function:

Coordination of an organisms activities

54
Q

Receptor proteins

A

Function:

Response of cell to chemical stimuli

55
Q

Contractile and motor proteins

A

Function:

Movement

56
Q

Structural proteins

A

Funtion:

support

57
Q

Enzymatic proteins act as catalysts to do what in a chemical reaction

A

to speed up chemical reactions without being consumed in the reaction

58
Q

Polypeptides

A

are unbranched polymers built from the same set of 20 amino acids

Amino acids are linked by peptide bonds

A polypeptide is a polymer of amino acids

Polypeptides range in length from a few to more than a thousand monomers

Each polypeptide has a unique linear sequence of amino acids, with a carboxyl end (C-terminus) and an amino end (N-terminus)

59
Q

Protein

A

A protein is a biologically functional molecule that consists of one or more polypeptides (chain of amino acids)

60
Q

Proteins structure and function

A

A functional protein consists of one or more polypeptides precisely twisted, folded, and coiled into a unique shape

The amino acid sequence of each polypeptide leads to a protein’s three-dimensional structure

A protein’s structure determines its function

61
Q

What are the four levels of protein structure?

A

Proteins are very diverse, but share three superimposed levels of structure called primary, secondary, and tertiary structure

A fourth level, quaternary structure, arises when a protein consists of two or more polypeptide chains

62
Q

Breifly describe the four levels of protein structure in order

A

The primary structure of a protein is its unique sequence of amino acids

Secondary structure, found in most proteins, consists of coils and folds in the polypeptide chain

Tertiary structure is determined by interactions among various side chains (R groups)

Quaternary structure results from interactions between multiple polypeptide chains

63
Q

Sickle-cell disease

A

A slight change in primary structure can affect a protein’s structure and ability to function

Sickle-cell disease, an inherited blood disorder, results from a single amino acid substitution in the protein hemoglobin

64
Q

What is Denaturation

A

In addition to amino acid sequence, physical and chemical conditions can affect protein structure

Alterations in pH, salt concentration, temperature, or other environmental factors can cause a protein to unravel

This loss of a protein’s native structure is called denaturation

A denatured protein is biologically inactive

65
Q

X-ray crystallography

A

It is difficult to predict a protein’s structure from its primary structure

Most proteins probably go through several intermediate structures on their way to their final, stable shape

Scientists use X-ray crystallography to determine
3-D protein stucture based on diffractions of an
X-ray beam by atoms of the crystalized molecule

66
Q

gene

A

The amino acid sequence of a polypeptide is programmed by a unit of inheritance called a gene

Genes are made of DNA, a nucleic acid made of monomers called nucleotides

67
Q

Name the two types of nucleic acids and describe what they do

A

There are two types of nucleic acids

Deoxyribonucleic acid (DNA)

Ribonucleic acid (RNA)

DNA provides directions for its own replication

DNA also directs synthesis of messenger RNA (mRNA) and, through mRNA, controls protein synthesis

68
Q

polynucleotides

A

Nucleic acids are polymers called polynucleotides

69
Q

Nucleotides what are they and what are their pairings

A

Each polynucleotide is made of monomers called nucleotides

Each nucleotide consists of a nitrogenous base, a pentose sugar, and one or more phosphate groups

The portion of a nucleotide without the phosphate group is called a nucleoside

Adeine to thynein

Cytosine to guinene

70
Q

Each nitrogenous base has one or two rings that include nitrogen atoms

There are two families of nitrogenous bases

name the and tell which ones go to DNA and which Go to RNA

A

Pyrimidines include cytosine (C), thymine (T), and uracil (U)

Purines include adenine (A) and guanine (G)

Thymine is found only in DNA, and uracil only in RNA; the rest are found in both DNA and RNA

71
Q

What is a nucleoside with at least one phosphate attached

A

A nucleoside with at least one phosphate attached is a nucleotide

72
Q

What is a double helix in a DNA molecule and what does antiparallel mean in this molecule

A

DNA molecules have two polynucleotides spiraling around an imaginary axis, forming a double helix

In the DNA double helix, the two backbones run in opposite 5¢→ 3¢ directions from each other, an arrangement referred to as antiparallel

One DNA molecule includes many genes

73
Q

The nitrogenous bases in DNA pair up and form hydrogen bonds:

Name them

A

adenine (A) always with thymine (T), and guanine (G) always with cytosine (C)

This is called complementary base pairing

74
Q

Genomics

A

Genomics is the approach used to analyze large sets of genes or compare the genomes of different species

75
Q
A
76
Q

Name all 20 amino acids

first the Nonpolar side chains

second the Polar side chains

and

last the electrically charged side chains (negative and positive)

A

Nonpolar side chains have nine

mnemonic

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Glycine, Alanine, Valine, Leucine, Isoleucine, Methionine, Phenylalanine, Tryptophan, Proline.

Polar side chains

mnemonic:

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Serine, Threonine, Asparagine, Glutamine, Cysteine, Tyrosine

Electrically charged

mneumonic:

Ass grab

Aspartic acid, and Glutamic Acid

Negative because girls dont like having their ass grabbed

mnemonic:

Lick All Holes

Lysine, Arginine, Histidine

All baisic girls like being licked

Postive outcome

Biology I (8 decks)

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