covalent and hydrogen bonds - ANSWER -covalent bonds form between
atoms in a molecule
-hydrogen bonds form between polar water molecules
-electrons spend more time near oxygen, more electronegative
-arrangement constantly changes, multiple hydrogen bonds at a time
hydrophobic interaction - ANSWER -hydrophobic substances are nonpolar
and repel water
-lipids in a water environment will attract each other, decreasing entropy
-molecules are more ordered near surfaces, when surface area decreases (lipids
group together), entropy decreases
polysaccharide structure-function - ANSWER -carbohydrate chains, polymers
of sugars, helix shape
-monosaccharides are joined by glycosidic linkage (covalent bond formed by
dehydration reaction
-glucose polymers include starch (plant storage, alpha linkages), glycogen
(animal storage), cellulose (plant structure, beta linkages), and chitin (animal
structure)
-hydrolysis breaks down polysaccharides for energy
lipid structure-function - ANSWER -fats consist of glycerol and fatty acids
(hydrophobic carbon skeleton)
-triacylglycerol has 3 fatty acids join to glycerol by an ester linkage
-saturated fats have maximum number of hydrogens, no double bonds, solid at
room temp
-unsaturated fats have double bonds, bends in the carbon chain, liquid at room
temp
-fats are great for energy storage, adipose tissue
-phospholipids have a hydrophilic head, hydrophobic tail
,-form phospholipid bilayer together, cell membrane
-steroid are soluble, have cyclical carbon structures, include cholesterol (in
animal cell membranes) and hormones
protein structure - ANSWER -amino acids have an amino, carboxyl, and
variable group
-polypeptides are polymers of amino acids, joined by peptide bonds
(dehydration reaction)
-amino acids are always added to the C-terminus
-primary structure is the sequence of amino acids, determined by genetic
information
-secondary structure is the coils and folds resulting from hydrogen bonds, alpha
helix or beta sheet
-tertiary structure is overall shape resulting from side chain interactions, held
together by hydrogen bonds, disulfide bridges (covalent), and ionic bonds,
hydrophobic collapse pushes nonpolar parts of the protein inward and decreases
surface area
-quaternary structure is the combination of tertiary proteins, hemoglobin is
made of 4 parts
nucleic acid structure - ANSWER -nucleotides have a nitrogenous base
(AGCTU), pentose sugar (deoxyribose, ribose), phosphate group
-pyrimidines are CTU, purines are AG
-double hydrogen bond between A and T/U, triple hydrogen bond between G
and C
-nucleotides are joined by phosphodiester linkage, covalent bond between sugar
of one and phosphate of the other
protein folding - ANSWER -chaperones are proteins that assist in proper
protein folding
-hydrophobic collapse is delayed by HSP60, HSP70, powered by ATP, keeping
proteins away from external influences
-HSP70 holds on and lets go
-HSP60 changes shape at same time, cooperativity
protein turnover - ANSWER -ubiquitin-proteasome system breaks down
misfolded proteins (30% of all proteins)
, -ubiquitin ligase (enzyme) attaches ubiquitin to the protein, signalling a
proteasome to come break it down with hydrolysis
ATP function - ANSWER -ATP hydrolysis (exergonic reaction, favored) is
coupled with protein synthesis (endergonic reaction, unfavored)
-ATPase (ex. HSP70) puts strain on ATP, Mg2+ holds other bonds in place,
water hydrolyzes, and a phosphate is released
-the phosphate is used to phosphorylate something
enzyme structure-function - ANSWER -proteins that catalyze metabolic
chemical reactions
-bind to specific substrates and lower the activation energy for a certain reaction
to occur
-active site, lock and key, induced fit
enzyme regulation - ANSWER -allosteric regulation involves some ligand
binding to the allosteric site, causing a conformation change of the enzyme
-covalent modification involves phosphorylation of the enzyme, phosphate
came from ATP
organelle functions - ANSWER -nucleus, nuclear envelope, nuclear lamina,
chromosomes/chromatin, nucleolus
-mitochondria, chloroplasts, etc.
-ribosomes are suspended in cytosol or attached to ER (make proteins that need
to be shipped somewhere)
-endomembrane system includes nuclear envelope, endoplasmic reticulum,
golgi apparatus, lysosomes, vacuoles, plasma membrane
-smooth ER does synthesis of lipids, metabolism of carbohydrates, detox of
drugs
-rough ER has ribosomes on it that feed their polypeptides into the ER lumen
-golgi apparatus modifies, sorts, and targets products to various pars of cell,
identification tags
-lysosomes are membranous sacs of hydrolytic enzymes that animal cells use to
digest molecules
-acidic environment inside
-phagocytosis is where a vacuole fuses with lysosome
-autophagy is where damaged organelles are surround by a membrane and
brought to lysosome
atoms in a molecule
-hydrogen bonds form between polar water molecules
-electrons spend more time near oxygen, more electronegative
-arrangement constantly changes, multiple hydrogen bonds at a time
hydrophobic interaction - ANSWER -hydrophobic substances are nonpolar
and repel water
-lipids in a water environment will attract each other, decreasing entropy
-molecules are more ordered near surfaces, when surface area decreases (lipids
group together), entropy decreases
polysaccharide structure-function - ANSWER -carbohydrate chains, polymers
of sugars, helix shape
-monosaccharides are joined by glycosidic linkage (covalent bond formed by
dehydration reaction
-glucose polymers include starch (plant storage, alpha linkages), glycogen
(animal storage), cellulose (plant structure, beta linkages), and chitin (animal
structure)
-hydrolysis breaks down polysaccharides for energy
lipid structure-function - ANSWER -fats consist of glycerol and fatty acids
(hydrophobic carbon skeleton)
-triacylglycerol has 3 fatty acids join to glycerol by an ester linkage
-saturated fats have maximum number of hydrogens, no double bonds, solid at
room temp
-unsaturated fats have double bonds, bends in the carbon chain, liquid at room
temp
-fats are great for energy storage, adipose tissue
-phospholipids have a hydrophilic head, hydrophobic tail
,-form phospholipid bilayer together, cell membrane
-steroid are soluble, have cyclical carbon structures, include cholesterol (in
animal cell membranes) and hormones
protein structure - ANSWER -amino acids have an amino, carboxyl, and
variable group
-polypeptides are polymers of amino acids, joined by peptide bonds
(dehydration reaction)
-amino acids are always added to the C-terminus
-primary structure is the sequence of amino acids, determined by genetic
information
-secondary structure is the coils and folds resulting from hydrogen bonds, alpha
helix or beta sheet
-tertiary structure is overall shape resulting from side chain interactions, held
together by hydrogen bonds, disulfide bridges (covalent), and ionic bonds,
hydrophobic collapse pushes nonpolar parts of the protein inward and decreases
surface area
-quaternary structure is the combination of tertiary proteins, hemoglobin is
made of 4 parts
nucleic acid structure - ANSWER -nucleotides have a nitrogenous base
(AGCTU), pentose sugar (deoxyribose, ribose), phosphate group
-pyrimidines are CTU, purines are AG
-double hydrogen bond between A and T/U, triple hydrogen bond between G
and C
-nucleotides are joined by phosphodiester linkage, covalent bond between sugar
of one and phosphate of the other
protein folding - ANSWER -chaperones are proteins that assist in proper
protein folding
-hydrophobic collapse is delayed by HSP60, HSP70, powered by ATP, keeping
proteins away from external influences
-HSP70 holds on and lets go
-HSP60 changes shape at same time, cooperativity
protein turnover - ANSWER -ubiquitin-proteasome system breaks down
misfolded proteins (30% of all proteins)
, -ubiquitin ligase (enzyme) attaches ubiquitin to the protein, signalling a
proteasome to come break it down with hydrolysis
ATP function - ANSWER -ATP hydrolysis (exergonic reaction, favored) is
coupled with protein synthesis (endergonic reaction, unfavored)
-ATPase (ex. HSP70) puts strain on ATP, Mg2+ holds other bonds in place,
water hydrolyzes, and a phosphate is released
-the phosphate is used to phosphorylate something
enzyme structure-function - ANSWER -proteins that catalyze metabolic
chemical reactions
-bind to specific substrates and lower the activation energy for a certain reaction
to occur
-active site, lock and key, induced fit
enzyme regulation - ANSWER -allosteric regulation involves some ligand
binding to the allosteric site, causing a conformation change of the enzyme
-covalent modification involves phosphorylation of the enzyme, phosphate
came from ATP
organelle functions - ANSWER -nucleus, nuclear envelope, nuclear lamina,
chromosomes/chromatin, nucleolus
-mitochondria, chloroplasts, etc.
-ribosomes are suspended in cytosol or attached to ER (make proteins that need
to be shipped somewhere)
-endomembrane system includes nuclear envelope, endoplasmic reticulum,
golgi apparatus, lysosomes, vacuoles, plasma membrane
-smooth ER does synthesis of lipids, metabolism of carbohydrates, detox of
drugs
-rough ER has ribosomes on it that feed their polypeptides into the ER lumen
-golgi apparatus modifies, sorts, and targets products to various pars of cell,
identification tags
-lysosomes are membranous sacs of hydrolytic enzymes that animal cells use to
digest molecules
-acidic environment inside
-phagocytosis is where a vacuole fuses with lysosome
-autophagy is where damaged organelles are surround by a membrane and
brought to lysosome
