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20 Cards in this Set

  • Front
  • Back
Nuclear Magnetic Resonance spectroscopy
atomic nuclei possess a property called spin; when placed in an external static magnetic field, the nuclear spin will precess around the axis of the external magnetic field at a specific resonance frequency known as the chemical shift.
nuclear Overhauser effect
the nuclei of individual atoms interact with one another in a way that can be correlated with the internuclear distance by which they are separated.
X-ray crystallography
The protein crystal is then irradiated with a high intensity X-ray beam, which is diffracted by the protein crystal to form a pattern of spots known as a diffraction pattern.
peptide bonds
amino acids are joined end-to-end by amide bonds between the alpha-amino group of one amino acid and the alpha-carboxyl group of another amino acid
primary structure
The sequence of amino acids in a protein
N-terminus
amino-terminal end of a polypeptide chain
C-terminus
carboxyl-terminal end of a polypeptide chain
The conformation of a polypeptide chain is partly constrained because
rotation around a peptide bond is prevented by the partial double bond character of this bond
groups lie in a plane
secondary structure
Helical and sheet structures formed from folded polypeptide chains
Protein secondary structures exist 1
only certain combinations of the backbone dihedral angles phi and psi eliminate steric clashes between backbone and sidechain atoms of adjacent amino acid residues.
Protein secondary structures exist 2
opportunities for hydrogen bond formation exist when polypeptide chains adopt helical and sheet conformations
alpha-helix
This structure can be represented by a right spiral staircase with amino acids for steps.
Side chains project away from the center.
Hydrogen bonds between the backbone amide group of an amino acid and the backbone carbonyl group of another amino acid four steps away stabilize the alpha-helix.
beta-sheet
One extended polypeptide chain (designated as a beta-strand) hydrogen bonds with another polypeptide chain (another beta strand) to form a beta-sheet.
Side chains project either above or below the beta-sheet.
often see branched sidechains
collagen helix
"stretched alpha-helix” which lacks intrastrand hydrogen bonds
Tertiary structure
the three-dimensional structure of a polypeptide chain.
stabilized by hydrogen bonds, electrostatic bonds, hydrophobic interactions and, in certain cases, disulfide bonds.
Disulfide bonds
by oxidation between the sulfhydryl groups of the side chains of cysteine residues that are in close spatial proximity
denaturation
The process of losing protein structure
denaturation reagents
break hydrogen bonds, such as urea and guanidine hydrochloride
renature
refold and become active if reagent is removed by dialysis
Quaternary structure
the arrangement of polypeptides in aggregates that have several polypeptides.