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Biology > Lecture 4 Chemical Bonds > Flashcards

Lecture 4 Chemical Bonds Flashcards

1
Q

Organic Molecules

A

contain carbon and hydrogen atoms

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2
Q

Biomolecules (Organic Molecules)

A

Carbohydrates
Lipids
Proteins
Nucleic Acids

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3
Q

Inorganic vs. Organic Molecules

A

Inorganic usually contain positive & negative ions, while Organic always contain Carbon and Hydrogen

Inorganic is usually ionic bonding, while Organic is always covalent bonding

Inorganic always contain a small number of atoms, while Organic is often quite large with many atoms

Inorganic is associated with non living matter, while Organic is associated with living organisms

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4
Q

Carbon

A

Shares well with elements

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5
Q

Functional Groups

A

clusters of specific atoms that always act the same way, bonded to the carbon skeleton with characteristic structures and functions

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6
Q

Isomers

A

organic molecules that have identical molecular formulas but a different arrangement of atoms. You would naturally expect these guys to react differently than one another in chemical reactions

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7
Q

Monomer & Polymer

A

Monomer- A repeating unit

Polymer- A Molecule composed of monomers

Ex: amino acids (monomer) are joined together to form a protein (polymer)

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8
Q

Dehydration Reaction

A

a chemical reaction in which subunits are joined together by the formation of a covalent bond and water is produced during the reaction

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9
Q

Hydrolysis Reaction

A

a chemical reaction in which a water molecule is added to break a covalent bond

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10
Q

Enzymes

A

a molecule that speeds up a chemical reaction

  • Enzymes are required for cells to carry out dehydration synthesis and hydrolysis reactions.
  • Enzymes are not consumed in the reaction.
  • Enzymes are not changed by the reaction.
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11
Q

Carbohydrates

A

•Functions:
●Energy source
●Provide building material (structural role)

  • Contain carbon, hydrogen and oxygen in a 1:2:1 ratio
  • Varieties: monosaccharides, disaccharides, and polysaccharides
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12
Q

Monosaccharide

A

a single sugar molecule

•Examples:
●Glucose (transported in blood, gets broken down & converted into ATP), fructose (fruit) and galactose
•Hexoses - six carbon atoms
●Ribose and deoxyribose (in nucleic acids RNA & DNA)
•Pentoses – five carbon atoms

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13
Q

Disaccharide

A

contains two monosaccharides joined together by dehydration synthesis.
•Examples:
●Lactose (milk sugar) is composed of galactose and glucose.
●Sucrose (table sugar) is composed of glucose and fructose.
●Maltose is composed of two glucose molecules.

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14
Q

Polysaccharide

A

A polymer of monosaccharides. These are often used as short-term energy storage molecules.
•Examples:
●Starch provides energy storage in plants.
●Glycogen provides energy storage in animals.
●Cellulose is found in the cell walls of plants (most abundant carbohydrate & organic molecule on earth)

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15
Q

Lipids

A 
•Lipids are varied in structure.
•Large nonpolar molecules that are insoluble in water
•Functions:
●Long-term energy storage
●Cell communication and regulation
●Protection

•Varieties: fats, oils, phospholipids, steroids, waxes

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16
Q

Triglycerides: Long-Term

Energy Storage

A

●Also called fats and oils
●Functions: long-term energy storage and insulation
●Consist of one glycerol molecule linked to three fatty acids by dehydration synthesis

17
Q

Unsaturated and Saturated

A

●Unsaturated - one or more double bonds between carbons
•Tend to be liquid at room temperature
–Example: plant oils

●Saturated - no double bonds between carbons
•Tend to be solid at room temperature
–Examples: butter, lard

18
Q

Phospholipids: form membranes (like cell membranes)

A

•Structure is similar to triglycerides
●Consist of one glycerol molecule linked to two fatty acids and a modified phosphate group
•Function: form plasma membranes
•In water, phospholipids aggregate to form a lipid bilayer.
●Polar phosphate heads are oriented towards the water.
●Nonpolar fatty acid tails are oriented away from water.
•Nonpolar fatty acid tails form a hydrophobic core.

19
Q

Waxes

A
  • Long-chain fatty acid bonded to a long-chain alcohol
  • Solid at room temperature
  • Waterproof
  • Resistant to degradation
  • Function: protection
  • Examples: earwax, plant cuticle, beeswax
20
Q

Proteins

A

•Proteins are polymers of amino acids linked together by peptide bonds.
●A peptide bond is a covalent bond between amino acids.

•Two or more amino acids joined together are called peptides.
●Long chains of amino acids joined together are called polypeptides.

•A protein is a polypeptide that has folded into a particular shape and has function.

21
Q

Functions of Proteins

A

•Metabolism
●Most enzymes are proteins that act as catalysts to accelerate chemical reactions within cells.
•Support
●Keratin (make up hair & nails) and collagen (gives strength to ligaments, tendons & skin)
•Transport
●Hemoglobin and membrane proteins transport oxygen to cells!
•Defense
●Antibodies
•Regulation
●Hormones are regulatory proteins that influence the metabolism of cells.
•Motion
●Muscle proteins (actin & myosin) allow muscle contraction & therefore movement!

22
Q

Levels of Protein Structure

A

•Proteins cannot function properly unless they fold into their proper shape.
●When a protein loses it proper shape, it said to be denatured.
•Exposure of proteins to certain chemicals, a change in pH, or high temperature can disrupt protein structure.

•Proteins can have up to four levels of structure:
●Primary
●Secondary
●Tertiary
●Quaternary
23
Q

Four levels of protein structure

A

●Primary
•The sequence of amino acids
●Secondary
•Characterized by the presence of alpha helices and beta (pleated) sheets held in place with hydrogen bonds
●Tertiary
•Final overall three-dimensional shape of a polypeptide
•Stabilized by the presence of hydrophobic interactions, hydrogen bonding, ionic bonding, and covalent bonding
●Quaternary
•Consists of more than one polypeptide

24
Q

Protein folding diseases

A

•Chaperone proteins help proteins fold into their normal shape.
●Defects in chaperone proteins may play a role in several human diseases such as Alzheimer disease and cystic fibrosis.
•Prions are misfolded proteins that have been implicated in a group of fatal brain diseases known as TSEs. (transmissible spongiform encephalopathies). Prions are hypothesized to cause other proteins to mis-fold as well, so they are kind of like bad influence proteins!

25
Q

Nucleic Acids

A

•Nucleic acids are polymers of nucleotides that store this information, including instructions for life, and conduct chemical reactions!

•Two varieties of nucleic acids:
●DNA (deoxyribonucleic acid)
•Genetic material that stores information for its own replication and for the sequence of amino acids in proteins.
●RNA (ribonucleic acid)
•Perform a wide range of functions within cells which include protein synthesis and regulation of gene expression

26
Q

Structure of a Nucleotide

A

•Each nucleotide is composed of three parts:
●A phosphate group
●A pentose sugar
●A nitrogen-containing (nitrogenous) base
•There are five types of nucleotides found in nucleic acids.
●DNA contains adenine, guanine, cytosine, and thymine.
●RNA contains adenine, guanine, cytosine, and uracil.
•Nucleotides are joined together by a series of dehydration synthesis reactions to form a linear molecule called a strand.

27
Q

Structure of DNA & RNA

A

●The backbone of the nucleic acid strand is composed of alternating sugar-phosphate molecules.
●RNA is predominately a single-stranded molecule.
●DNA is a double-stranded molecule.
•DNA is composed of two strands held together by hydrogen bonds between the nitrogen-containing bases. The two strands twist around each other to form a double helix.
–Adenine hydrogen bonds with thymine
–Cytosine hydrogen bonds with guanine
•The bonding between the nucleotides in DNA is referred to as complementary base pairing.

28
Q

DNA structure compared to RNA structure

A

DNA has deoxyribose sugars and is double stranded while

RNA had ribose sugars and is single stranded

29
Q

A special Nucleotide: ATP

A

•ATP (adenosine triphosphate) is composed of adenine, ribose, and three phosphates.
•ATP is a high-energy molecule due to the presence of the last two unstable phosphate bonds.
•Hydrolysis of ATP yields:
●The molecule ADP (adenosine diphosphate)
●An inorganic phosphate
●Energy to do cellular work
•ATP is called the energy currency of the cell.

Biology (5 decks)

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