Biochem Final part 1 Flashcards
Hydrophobic
water-fearing
hydrophobic effect
the energetic preference of nonpolar molecular surfaces to interact with other nonpolar molecular surfaces and thereby to displace water molecules from the interacting surfaces
Hydrophilic
water-loving
Amphoteric
they can react either as acids or bases, depending on the circumstances
Isoelectric point
the pH at which the net electric charge is zero
zwitterion
a functional group molecule in which at least one has a positive electrical charge and one a negative electrical charge.
primary structure
covalent bonds linking amino acid residues in a polypeptide chain
secondary structure
recurring structural patterns
-ɑ-helix, β-sheets, β-turn, random coils
tertiary structure
3D folding of polypeptide
-determined by amino acid sequence
-hydrogen bonds between nearby amino acid residues
- salt bridges
quaternary structure
2+ polypeptide subunits
protein domain
part of a polypeptide chain that is independently stable or could undergo movements as a single entity
motif
recognizable folding pattern involving 2+ elements of 2° structures & the connection(s)
b-a-b loop or b barrel
Intrinsic disorder proteins
-Lack of definable structure
-Often lack a hydrophobic core
-High densities of charged residues (Lys, Arg, Glu) and Pro
-Facilitates protein interactions with multiple binding partners
Denaturation
loss of three-dimensional structure sufficient to cause loss of function
- can happen by heat, pH extremes, detergents, strong acids/bases, organic solvents
native conformation
the arrangement of all atoms contained in the protein in a conformation that is stable and functional
thermodynamically the most stable, therefore, lowest free energy