biochemistry Flashcards
What are the 4 functional groups and what do they do?
OH (hydroxyl) - in carbohydrates and alcohols
COOH (carboxyl) - fatty acid/and in amino acids
NH3 - amino group
PO4 (phosphate) - in nucelic acids
What is a condensation reaction?
When organic molecules are bonded and water is a byproduct (water in released during the reaction) also known as dehydration
(to undo hydrolysis/add water)
What are the different proteins structures?
Primary - sequence of AAA
Secondary - some repel some attract (alpha helix and beta pleat)
Tertiary- 3D arrangement of secondary structure (cuz of bonds)
Quaternary - 2+ polypeptides combined (may or may not happen)
Types of covalent bonds (2)
Non polar: sharing electrons evenly - hydrophobic/lipophillic
Polar: sharing elections unevenly (overall charge) - hydrophilic/lipophopic
Life is _________ based
Carbon
What is “the ability to take away e from other atoms?
Electronegitivity
Uses of carbohydrates (and some sources?)
Uses: energy, plant cell walls, exoskeleton of insects, etc.
Sources: bread, grains, potatoes, sugars, cellulose, etc.
Uses of proteins? (7)
Structure (nails, collagen, bones, hair)
Muscle (movement)
Transport of o2 (hemoglobin)
Hormones
enzymes
Cell communication
Antibodies
Differences and similarities between cellulose and starch?
Both are polysaccharides
Cellulose:
- energy storage in plants
- beta 1,4 glycosidic bonds
-monosaccharides flip each time (cuz of shape)
Starch:
- energy storage in animals
- alpha 1,4 glycosidic bonds
saturated fats vs unsaturated fats (cis vs trans)
saturated: all carbons are connected by single bonds (very dense - you can stack them together/solid at room temp)
unsaturated (essential for humans): contain at least 1 double bond between carbons (liquid at room temp)
- cis : both hydrogen atoms located on the same side of double bond
- trans fatty acids have the two hydrogen atoms on opposite sides of double bond
denaturation of h bonds (explain)
heat or extreme cold can break h-bonds which alters the structure of the protein/enzyme/etc. the proper function may not be achieved if this is the case
(denaturation can also be caused by bases, acids or lots of salt)
enzymes (structure, function)
enzymes are organic catalysts that facilitate chemical reactions. a substrate is anything an enzyme works on and therefore they have a shape the is specific to their substrate (induced fit)
allosteric site: on/off switch
active site
how are enzymes regulated (4)
competitive inhibition: compete for active site (other substrate with similar shape, high concentration)
non comp inhibition: does not invovle the active site
- allosteric: allosteric site (shape change)
- feedback; high levels of product has backward effect (inhibits enzyme that catalysts the first or one of the first reactions in a series)
enzyme optimum is based on two factors?
pH (ex. pepsin has pH optimum 1-2)
temperature (so that enzyme has right shape)
what is a phospholipid?
glycerol + Pi (& R group) + 2 fatty acids
hydrophilic end: glycerol + Pi (& R group: variable attachement)
hydrophobic end: fatty acids
- make up cell membrane