Chapter 3 Flashcards
Use of proteins
structure, enzymes, transport, signaling molecules
postive
hydrophilic
negative
hydrophilic
no charge
hydrophobic
Primary structure
long chain of amino acids
secondary
alpha helix and beta strands
tertiary
disulfide bridges, cystine molecules connected by side chains
quaternary
hemoglobin, 4 subunits come together
Cys Cys disulfide bridges
make up structure
hydrophobic forces
important for structure through interactions of non polar substances in the presence of polar substances
hydrogen bonds
structurally important by sharing H- atom- 2 polar groups
denaturing
death of a cell
nomenclature
mono, di, poly
mono
individual carb monomers
glucose and fructose
dis
2 monos covalently bonded together, alpha and beta
poly
3 glycosidic linkages
glycogen, starch
sugar phosphates
modify carbs
glucosamine
modify amino group
physical properties of fats
neutral, hydrophobic
triglycerides
(mono and di) the synthesis of an ester linkage releases water
saturated fats
chain of carbons, h saturated, linear
unsaturated fats
missing h, double covalently bonded
sterols
cholesterol is important for the body because it is a constituent of membranes and it is a source of steroids
