Unit 1: Biochem - Macromolecules Flashcards
6 Functions of proteins
Repair/Maintenance Transportation/Storage Energy Hormones Enzymes Antibodies
Peptide Bond
- Carboxyl group on one reacts with amine group, releasing water molecule
- Only found between amino acids
Primary structure
Specific sequence of AA’s, determined by nucleotides
Secondary structure
- α helix/β pleated sheet
- Three dimensional structure of a polypeptide chain -
- Formed by H bonds between amine group of AA, carboxyl group of other
Motifs
Recognizable combinations of secondary structure
Tertiary Structure
Final folded shape of polypeptide, formed by interactions between R groups
Disulfide bridges
Disulfide bridges
- Sulfhydryl groups of two cysteine monomers are brought closer together by the folding of the proteins
- Sulfur of one cysteine bonds to the sulfur of the second
Quaternary structure
- Aggregation of two polypeptide subunits
Denaturation
Unfolds proteins
Breaks s-s bonds, h-bonds, LDF’s, ionic bonds via HYDROLYSIS
Chaperonins
Folds misfolded proteins using ATP
ENVIRONMENTAL causes of denaturation
Heat
pH - H+ sticks to R groups messes up charge of amino acid
Salt - Same
Solvent - Non polar solvents screw up hydrophilic/hydrophobic ends
Carb Basics (Function, structure)
CH2O
- Short term energy storage (4 kCal/gram)
Glycosidic Linkages
- Between two monosaccharides
- Uses dehydration synthesis
- α 1-4 linages, α 1-6 linkages
Structural Isomers
Different atoms connected (most different of isomers)
Glucose-Aldose + Fructose-Keytose
Stereoisomers
Geometric/Enantiomers
Stereo isomers - Same atoms connected, different shape
Geometric - Have double bonds, or rings
Enantiomers - Mirror Images
Chiral Carbon
carbon atom that is attached to four different types of atoms or groups of atoms
Starch basics
Function, Properties, Structure
- Short term energy storage in plants
- Polar + Hydrophilic
- Not soluble because or size
- instead, amylase hydrolyzes alpha 1-4 bonds in starch
Short term energy storage in animals
Glycogen
Liver + muscle
Cellulose basics
Function, Structure
- Found in plant cell walls and algae
- Monomer is B glucose (OH above C)
- Flipping glucose allows for hydrogen bonding between forming lattice
Cellulose is broken down by
Cellulase - breaks B 1-4 bonds, leaving us with glucose!
Fiber
Undigested cellulose!
Chitin
- Structure in arthropod exoskeletons, fungi, cell walls
- Monomer - N-acetyl glucosamine
- B bonds 1-4, H bonds, and others between linear chains
Peptidoglycan
- Bacterial/Prokaryote cell walls
- CHN Monomer with cross linked peptide chain attached
Lipid Basics
Structure, Properties
C, H, O, Sometimes P
- Non-polar, don’t dissolve in water
Fats
Functions, structure
- Triacylglycerols/Triglycerides
- Long term energy storage - 9kcal/g
- Insulation and cushioning
- 3 Fatty acids + glycerol through ester linkage
- Common in animals, some plants (avocados, seeds)
Why do fats have so much energy?
- Non-polar bonds are stable, hard to break, release a lot of energy
- More energy and weigh less than carbs bc of molecular formula
- Always more H than O, H weighs less 1:16
Monomer of a lipid
NO MONOMER OF A FAT LIPID
Ester linkage
Dehydration synthesis to bond glycerol to fatty acid
leaves O and CO
Saturated
No double bonds, max number of H, STICKS
Unsaturated
At least one double bond along fatty acid chain, fewer H
Fatty Acids
12-20 carbons long
3 fatty acids per fat molecule
Omega
C=C closest to the left
Essential fatty acids - must be consumed cause your body can’t make a bond in that specific place
Fats = Fatty acids?
NO
fats are larger, more LDF’s hold together better
Trans Fats
- People wanted spreadable oils - hydrolyze oils to make solid
- Trans configuration
Hydrolization
Addition of hydrogen to make unsat - sat
Cis/Trans
Cis - Functional group on same sides of carbon chain
Trans - Functional group on opposing sides
Phospholipids
- Make up membranes
- Hydrophobic tail / Hydrophilic Head
- Head is phosphate group and glycerol
- One unsaturated fatty acid tail, one saturated
- Tails connected by ester bonds
Amphipathic
One part hydrophobic, One hydrophilic
Steroids
- 3 Hexagons, one pentagon, made of C + H
- Non-polar
- Rigid
- Each defined by their chemical structure
Cholesterol
- Precursor for other steroids
- In plasma membranes for structure
Last group of lipids
Not fats, phospholipids, or steroids,
Terpane (citronella)
Nucleic Acid Basics
Structure, Functions
CHONP
- Monomer: Nuctleotides joined by phosphodiester bonds
- Catalyze reactions as RNA
- Energy transfer - ATP
- Structural purposes
Nucleotide
Phosphate group, pentose, nitrogenous base
Phosphodiester bond
Dehydration synthesis between phosphate group and 3 carbon
Purines/Pyrimidines
Purines - Double ring - Adenin, Guanine
Pyrimidines - Single ring - Cytosine, thymine, Uracil
Nitrogenous base bonds
A = T/U C = G
Strand 5 VS. 3
- Phosphate group on strand 5
- Hydroxyl group on strand 3
- Oxygen always points towards 5
RNA
- Ribose, ACGU, single stranded, inconsistent shape
- Can h bond if in correct shape (TRNA)
rRNA - Ribosomes
Ribozymes - Catalyze reactions
mRNA - Transfer of info
DNA
- Deoxyribose, ACGT, double helizz
- 2 polynucleotide strands, held together by H bonds
- 3 rings, keeps consistent shape
Why is DNA strand antiparallel?
A + T have h bonding pairs that fit, but only if one is flipped, thus DNA strands run anti parallel
What is always slightly positive in an H bond?
H
ATP
- Adenosine Triphosphate
- Nitrogenous base + pentose + 3 phosphate groups
- ENERGY TRANSFER
- Bond between phosphate - Phosphoanhydride
Nucleoside
Nitrogenous base + pentose
Why does ATP supply so much energy
- Negative charges on O- repel each other, making molecule unstable, easy to break
- Releases small amounts of energy, but accessible
NAD+
- Nicotinamide Adenine Dinucleotide
- Because of opposite charge, molecule picks up ATP, goes back and forth depending on surroundings
- Performs redox reactions
Redox reactions
Transfers electrons between molecules
