Ch 3 Chemical Building Blocks Flashcards
Stereoisomers
Differ in how molecular groups attach
Isomers
Molecules with the same molecular or empirical formula
Enantiomers
Mirror image molecules
Ex: OH and HO
Polymer macromolecules
Built by linking monomers
Monomer
Small, similar chemical subunits.
Dehydration synthesis
Formation of large molecules by the removal of water
Responsible for turning monomers into polymers
Hydrolysis
Breakdown of large molecules by the addition of water
- responsible for breaking down polymers into monomers
Carbohydrates
Molecules with 1:2:1 ratio of carbon, hydrogen, oxygen
CH2O
Is a polymer
Monosaccharides
Simplest carbohydrate
Good example-Glucose- c6h12o6
Fructose- structural isomer of glucose
Galactose-stereoisomer of glucose
Disaccharides
2 monosaccharides linked together by dehydration synthesis
Used for sugar transport or energy storage
Examples sucrose, lactose, maltose
Polysaccharide
Long chains of monosaccharides
Linked though dehydration synthesis
Energy storage- plants use starch. Animals use glycogen
Structural support- plants use cellular
Fungi use chitin
Nucleic acid
Polymer- Nucleic acids
Monomers- nucleotides
Sugar + phosphate + nitrogenous base
Sugar is deoxyribose in DNa or ribose in rna
Phosphodiester bonds
This connect nucleotides together
Dna
Deoxyribonucleic acid
Encodes information for amino acid sequence of proteins
Double helix
2 polynucleotide strands connected by hydrogen bonds
A-----t = always double hydrogen bond C----g = always triple hydrogen bond
Rna
Ribonucleic acid
Contains uracil instead of thymine
Single polynucleotide strand
Uses information in Dna to specify sequence of amino acids in proteins.
Make up amino acids
Atp
Adenosine triphosphate
Primary energy currency of the cell
Proteins functions
Enzyme catalysis Defense Transport Support Motion regulation Storage
Proteins
Are polymers. Composed of amino acids
Primary structure of protein
Sequence of amino acids to form polypeptide
Secondary structure of protein
Folding of polypeptide due to attraction and repulsions
Tertiary structure of protein
Final folded shape of a globular protein
– final level of structure for proteins consisting of only a single polypeptide chain
Attraction and repulsions of r groups
Quaternary structure of protein
Arrangement of individual chains (subunits) in a protein with 2 or more polypeptide chains.
Chaperones
Chaperone proteins help protein fold correctly.
Deficiencies in chaperone proteins cause disease like cystic fibrosis
Denaturation
Protein loses structure and function due to ph, temp, or ionic concentration of solution.
Lipids
Loosely defined group of molecules with one main chemical characteristic.
Insoluble in water.
High proportion of non polar c-h bonds causes the molecule to be hydrophobic.
Triglycerides
Composed of 1 glycerol and 3 fatty acids
Phospholipids
Composed of glycerol and 2 fatty acid
non polar tails.
Polar head
Phospholipid bilayer
More complicated structure where 2 layers form.
Hydrophilic heads point outwards
Hydrophobic tails point towards each other.
Nucleotide
Make up DNa strand
Made of phosphate, carbon, sugar, nitrogen