Molecules & Fundamentals of Biology Flashcards
What type of bonds do carbohydrates make?
Glycosidic bonds
**these are joined by dehydration in disacc. (condensation reaction)
What is the opposite of a dehydration reaction and what is the result?
Hydrolysis
Covalent bond is broken by the addition of water
What reaction results in a glycosidic bond?
Dehydration (condensation reaction)
Water molecule leaves, covalent bond is formed
What type of bonds do proteins make?
Peptide bonds
What type of bonds do lipids make?
Ester bonds
What type of bonds do nucleic acids make?
Phosphodiester bonds
Atoms making up carbs
CH2O (Carbon & 1 water)
Atoms making up proteins
CHON
Atoms making up lipids
CHO
Atoms making up nucleic acids
CHONP
What are Monosaccharides? What are the important ones?
One sugar
Ribose: 5C
Fructose: 6C
Glucose: 6C
What is maltose
glucose+glucose
Polypeptides
Polymer of amino acids
Joined by peptide bonds via dehydration synthesis(same as carbs)
Are broken apart via hydrolysis reactions
Chain has N- (amino) and C- terminus (carboxyl)
Primary Protein Structure
Amino acid sequence
- connected through peptide bonds
Secondary Protein Structure
Peptide backbone with IMFs - forms alpha helices & beta pleaded sheets
Tertiary Protein Structure
- R-group interactions of side chains into 3D structure
- R-groups create hydrophobic interactions
(Disulfide bonds/hydrogen bonds)
Quarternary Structure
- Multiple polypeptide chains, forces same as tertiary
Denaturation of proteins
- Loss of function & higher order structures
- ONLY PRIMARY structure UNaffected
Affected by: - pH changes
- Temperature changes (high or low)
- Salt concentrations
- Chemicals or radiation
Glycoprotein
proteins that contain a carbohydrate group
Metalloproteins
proteins that contain a metal ion cofactor
What do catalysts do?
Reduce the energy of the transition state
Do not shift a chemical reaction or affect spontaneity
Lowering the activation energy
Competitive inhibition
Inhibitors compete for active sites
Adding substrate can overcome this type of inhibition
Noncompetitive Inhibition
Non-competitive inhibitor binds to allosteric site modifies active site
*Rate of enzyme action cannot be increased by adding more substrate
*Cannot be overcome by adding more substrate
*Substrate and inhibitor don’t “compete” for active site
allosteric inhibition
Enzyme conformation changed by binding of inhibitor/activator to different site than active site
Factors that influence membrane fluidity
Temperature
Cholesterol
Degrees of Unsaturation
Metabolism
Conversion of food into form of energy our body can use
Metabolic pathways
product (end result) of earlier rxn serves as reactant (start) of future reaction
Catabolic
Breaks down
Releases energy (creates ATP)
Spontaneous rxns
EXERGONIC