Biochem- Macromolecules and General Principles of Proteins Flashcards
Primary structure or Proteins, types of stabilizing bonds
linear sequence of AA’s in a peptide, stabilized by peptide bonds ( includes disulfide bonds)
secondary structure of proteins, types of stabilizing bonds
local structure of nonbonding AA’s, stabilized with H bonding, includes alpha helices and Beta sheets
tertiary structure of proteins, types of stabilizing bonds
further folding of protein onto itself, forms 3 dimensional shape, stabilized by hydrophobic interactions, acid-base interactions (salt bridges), H bonds and disulfide bonds
quaternary structure of proteins, types of stabilizing bonds
2 or more protein chains bonded together by peptide bonds ( noncovalent bonds)- protein has multiple subunits
what amino acid forms disulfide bonds?
2 cysteine molecules are oxidized and create a covalent bond
How does proline affect protein structure?
disrupts secondary structures
what is denaturation?
loss of 3 dimensional structure ( tertiary), inactivates protein
what type of reaction forms a peptide bond?
condensation / dehydration
what type of reactions breaks a peptide bond?
hydrolysis
what is a peptide (amide) bond?
bond between carboxyl group of one amino acid and the amino group of another amino acid
How many carbons are in a pyranose CHO ring?
6
how many carbons are in a furanose CHO ring?
5
which type of chiral naming system is used for sugars and carbs?
L- D system
How can you tell if 2 sugars are enantiomers? what are their configurations?
D- and L- forms of the same sugar= enantiomers
what are diastereomers?
nonsuperimposable configurations of molecules with similar connectivity, differ at at least one, but not all chiral carbons