proteins Flashcards
amino acids
the building blocks of protein
how many different amino acids are there?
20
what is another name for ampholyte/amphoteric?
zwitterion
polypepetide chain
protein chain of less than 40-50 amino acids
what is another name for polypeptide chains?
residues
when does a polypeptide become a protein?
when there are 40-50 or more polypeptides
what kind of bond are peptide bonds?
covalent bonds
peptide bond characteristics
partial double bond, uncharged but polar
what type of isomer does fatty acids favor (cis/trans)?
cis favored
what type of isomer does amino acids favor (cis/trans)?
trans favored
primary structure of proteins
peptide bonds, connect 1 amino acid to another, short + no rotation
secondary structure of proteins
regular repeating local structures. stabilized by hydrogen bonds. contain alpha-helix, beta-sheets + triple-helix
tertiary structure of proteins
3-D structure formed by assembly of secondary structures
quaternary structure of proteins
structure formed by more than 1 polypeptide chain. contains all bonds
primary structure characteristics
sequence of amino acids. written left to right. starts with n-terminal amino acid + ends with c-terminal amino acid
secondary structure characteristics
organized compact structure of primary proteins
alpha-helix
spiral structure, tightly packed, polypeptide backbone, high tensile strength
beta-sheets
polypeptide chain arranged side by side, hydrogen bonds, fibrous protein, pleated look, parallel/antiparallel structure
triple-helix
3 polypeptide chains woven, hydrogen bonds
examples of triple-helix
collagen! glycine, proline, hydroxyproline, hydroxylysine
tertiary structure
cross links between R groups of secondary amino acids in chain
quaternary structure
folded proteins bind together to form dimer/trimers. 4 polypeptide chains
what is the functional form of hemoglobin (quaternary structure)?
tetramer
what are the bonds of the backbone + side chains of proteins?
covalent bonds
what bond maintains secondary, tertiary, + quaternary structures?
non-covalent bonds
hydrophobic AA
residues cluster in interior of globular proteins
hydrophilic AA
face the exterior of a structure or toward water
chaperones
proteins that assist the non-covalent folding/unfolding and the assembly/disassembly of other macromolecular structures
protein turnover
constant synthesizing/degrading, allowing removal of abnormal or unneeded proteins
ubiquitin-protease mechanism
proteins synthesized in the cell
degradative enzymes
acid hydrolases of the lysosomes
denaturation
disruption of secondary, tertiary, + quaternary proteins by heat/organics, acids/bases, heavy metal ions, + agitation