Lecture One. Flashcards
Most macromolecules are broken apart by ____
and formed by ____
Hydrolysis , Dehydration
Hydrolysis
Breaking a bond by adding the H and OH of water to either end.
Dehydration
Two molecules are combine to form a large molecule and water is formed as a by product.
Lipids Play Roles in :
Energy Storage , Cellular Organization and Structure in the membrane , start of vitamins and hormones .
Fatty Acids:
act as fuel for the body and are components of the membrane.
Triacylglycerols (Fats):
Function to store energy and to provide thermal insulation and padding.
Amphipathic
molecules that have a polar and nonpolar end.
Steroids
Regulate metabolic activities
The Liver Regulates
the blood glucose level
Plants Use _____ for long term storage
Starch ( amylose and amylopectin)
For plants Cellulose is Used
for structure and not energy , non-digestible in humans
Nucleotides are made up of …
Five carbon (pentose) sugar , a nitrogenous base, and a phosphate group.
Nucleotides are joined together by
phosphodiester bonds between the phosphate group of one nucleotide and the third carbon of the pentose sugar of the other nucleotide ( sugar-phosphate back bone)
Purines
Adenine and Guanine ( Two ring structures)
Pyrimidines
Cytosine and Thymine ( Single ring structures)
The Structure of RNA
Hydoxyl group attached to sugar, single stranded , contain uracil, and isn’t confined to the nucleus like DNA.
Amino Acids are linked by ________ to create protiens
Peptide bonds
Primary structure
the number and sequence of amino acids in a polypeptide
Secondary structure
alpha-helix and beta-sheet structures contribute to the overall shape, conformation, of the protein
tertiary structure
refers to the three dimensional shape formed by curls and folds in the peptide chain
quaternary structure
when two or more polypeptide chains bind together
Vmax is….
the maximum reaction rate of a enzyme, proportional to the enzyme concentration
Km is….
the substrate concentration at which the reaction rate is equal to 1/2 Vmax. indicates how highly concentrated the substrate must be to speed up the reaction.
Competative inhibitors…
compete with the substrate by binding to the active site, increase substrate (km) but not Vmax.
uncompetative inhibitors …
bind at a site other than the active site once the enzyme-substrate complex is formed. Vmax is lowered and Km is unaffected because adding more substrate doesn’t over come the inhibitor.