Biochemistry Flashcards
Hydroxyl Group
- OH ending
- Alcohols (“-ol”)
Carbonyl Group
=O
- Aldehydes (terminal) “-al”
- Ketones (non-terminal) “-one”
Carboxyl Group
- COOH
- Carboxylic acid “-oic acid”
- terminal
Amino Group
- NH2
- Amines “amine”
Sulfhydryl Group
- SH
- Thiols (“‘thiol”)
i. e. ethanethiol
Phosphate Group
- PO4
- Organic phospate (“phospho-“) prefix
i. e. phosphopropane
Organic Molecules
- Carbon as primary element
- Usually long and complex
Inorganic Molecule
- Carbon not primary ingredient
- Usually small and simple
Polar Bonds
-Atoms have unequal sharing of electrons
Non-polar bonds
-2 atoms with same/similar EN
Glycosidic Linkage
- 2+ carb monomers link together in condensation rx to form polysaccharides
i. e. glucose + glucose -> maltose
Ether Bond
- Condensation b/w two alcoholsbombines
i. e. ethanol +propanol -> ethoxypropane
Ester Bond
- Condensation b/w alcohol and organic acid
i. e. methanol + ethanoic acid -> methylethanoate
Peptide Bond
-Condensation rx b/w 2 amino acids
Disulphide Bond
- thiols combine
Phosphodiester Bond
- Phosphate in condensation rx with alcohol group on separate organic molecules
- Links nucleotide monomers
Carbs
- Short term energy storage
- All are aldehyde/ ketones
- “ose” usually
Alpha linkage
-Hydroxyl group points down
a+ a = down
Beta linkage
-Hydroxyl group points up
beta +beta = up
Polysaccharides
- Contain many units of glucose
i. e. starch, glycogen, cellulose, chitin - branched chain - glycogen, amylopectin
- straight chain- amylose
Glycogen
- Made of amylose and amylopeptin
- Energy storage in animals
- Glucose stored as glycogen when not in use
Starch
- Glucose units facing same direction (weaker bonds)
- Can be digested
- Soluble
Cellulose
- Glucose units facing different direction (stronger bonds- good for building)
- Can’t be digested
- Insoluble
Insulin
-lowers blood sugar level, tells cells to absorb glucose
Glucagon
-Raises blood sugar level, tells liver to release glucose
Lipids
- Not true polymers
- Lots of H
- Long term energy storage (Primary function)
- Protection and cushioning
- Structure (cell membrane)
- Signalling (enzymes)
Fats/Oils
Subunit- triglyceride (glycerol with 3 fatty acids)
- ester linkage
- Bent if contain double bond (creates irregular shape, more space b/w molecule, therefore liquid)
Saturated Fats
Single bonds only
Straight
Solid at room temp
Found in animals
Unsaturated fats
One or more double bonds
Liquid at room temperature
Found in plants
Trans Fats
Hydrogens on opposite sides of double bond
Cis Fats
Hydrogens on same side of double bond
Phospholipid
Phosphate group replaces third fatty acid
Hydrophillic head, hydrophobic tail
Heads face in, tails face out
Creates membranes in all living things (including organelles)
Steroids
4 carbon rings
- Makes cell membrane fliud/flexible
- Cholesterol- needed in small doses- make hormones, stabalizes cell membranes
Waxes
Protective coating/cover
Proteins
- Makes up most structures in cell, carry out chem processes (enzymes)
- Monomer is amino acid
Amino acid
Contains carbox acid group, amino group
20 different a.a.
Body can make 12, other 8 considered essential b/c must be in diet
linked by peptide bonds
Denatured
3-D shape of protein changed
protein no longer functional
Caused by high temp, extreme pH, reactive chemicals (i.e. Cl)
Protein Folding
1) Primary Structure- amino acids form polypeptide
2) Secondary Structure- Polypeptide folds into double helix or beta pleated sheet b/c of H bonds
3) Tertiary Structure- double helices and beta pleated sheets fold on themselves (charges groups attracting, hydrophillic/phobis interactions, disulphide bridges form and stabalizes 3D shape
4) Quanternary Structure- Multiple tertiary folded proteins come together to form one big unit i.e. hemoglobin
Nucleic Acid
Chemical codes store plans for all living things
DNA, RNA
Monomer- Nucleotide
Nucleotide
5 C sugar (ribose), phosphate, N base
link together with 3,5-phosphodiester linkage
Metabolism
Sum of all chem reactions in cell
Anabolism- small to big
Catabolism- big to small
Enzymes
Protein molecules that are biological catalysts
Very specific, hundreds/thousands of different enzymes
-“-ase” i,e lipase
Substrate- molecule that enzyme reacts with
Usually part of long series of linked reactions called metabolic pathway (i.e. photosynthesis)
3D shape determines activity
Region that substrate fits in is active site
Induced Fit Model
Active site conformed to the substrate, substrate and active site binds with H bonds
Brings a.a. closer to substrate, stresses bonds in substrate, Ea decreases OR adds/removes H+ atoms and acts as a catalytic acid or base
Temperatue and Enzymes
Functions best at 35-40 degrees for humans
Increase temp- H bond disturbed, shape/ function reduced, disulphide linkage break, protein denatured
Decrease temp- Become more rigid, less able to conform, function reduced
Exception: thermostable exzymes in bacteria in hot deep sea vents resistant to high temp. Used in industry
pH and Enzymes
Works best at 6-8 (humans)
Exception- pepsin, works best at 2-3
pH can denature enzyme (H bonds disrupted)
Specific pH creates correctly shaped active site
Slight change- function reduce
Extreme changes- denatures, loss of function
Cofactors
Non protein componenents needs for some enzymes for function
Bind to active site with covalent bonds, bind weakly with substrate
Coenzymes
Organic non protein cofactor
Derivative of vitamin
Carry molecules from one enzyme to another
Competitive Inhibitors
Substances that look like substrate and prevent substrate from binding to active site
Non competitive inhibitor
Attatches to somewhere other than active site and changes shape of active site
Allosteric inhibitor
Attahces at allosteric site and stabalizes inactive form of enzyme
Allosteric activator
Stabalizes protein conformation
keeps active site open
