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18 Cards in this Set

  • Front
  • Back

Native state:

afolded, biologically active protein in aconformation with the least free energy

Side chains:

project form the polypeptide backbone


Not involved in forming peptide bonds


Gives amino acid its unique properties

urea

denatures proteins by interfering with H bonding

Chaperone proteins:

bindto partly folded chains and help them fold along the most energeticallyfavourable pathway

Denaturation:

extremeconditions cause unfolding ( eg. pH,high temp)


Involvesthe disruption and or destruction of the secondary and tertiary structures

Prion:

abnormal misfolded protein that can bind tothe normal form and take over the cell and near by ones and cause death

Alpha helices:

carbonylis linked by a hydrogen bond to the N-H of a residue located 4 residues down the chain


Sidechains project outwards - no interior space


3.6 residues per turn, 0.54 nm per turn


keratinin hair

Proline

causeskinks


contains a ring that constrains bond angles so that it will not fitexactly into an α helix or β sheet

Coiled-coil:

twoor three a helices will wrap around one another


Repeatingpattern every 7 residues


Every1 and 4th position is hydrophobic and 5 and 7th is usually charged

Beta helices:

Twoor more separate polypeptide chains OR a single polypeptide folding back onitself


Sidechains project alternately up and down


Silkfibroin

parallel B sheet:

neighbouringsegments run in the same orientation

Antiparallel B sheet:

neighbouringsegments run in the opposite direction

Primary structure:

aminoacid sequence


Onlydeals with covalent bonds ( peptide ) linking residues together



Secondary structure:

folds eg.Alpha or beta helix


Involveshydrogen bonds between N-H and C=O groups

Tertiary structure:

threedimensional conformation


Formedfrom many weak noncovalent bonds betweenside chains or side chain to backbone

Disulfide bonds:

do not change proteins conformation but reinforce the most favourable conformation


canjoin either two parts of the same polypeptide chain or two differentpolypeptide chains.


Formbetween adjacent cyteine side chains


Onlyform in oxidizing environments



Protein domain:

any segment of a polypeptide chain that can foldindependently into a compact, stable structure


protein can have many or just one

Quaternary structure:

protein molecule forms a complex with morethan one polypeptide chain