None of the above
Shape and charge complementarity exclusively explain the interactions between an antibody and its target antigen.
Shape complementarity refers to the intimate contact made between an antibody and its target antigen.
(i) Charge complementarity occurs when specific non‐covalent binding interactions occur between two contacting surfaces
The "charge" interactions can be charge‐charge, H-bonding,or van der Waals interactions.
Protein X can be separated from protein C by specific affinity chromatography using immobilized DNA.
Protein X can be separated from protein A by size exclusion chromatography.
Protein X can be separated from protein B using ion-exchange chromatography.
Protein X can be separated from protein C by isoelectric focusing.
pK of His β146 is lowered as salt bridge to Asp β94 is broken.
Binding of O2 causes the heme to become more planar. This change brings the F helix closer to the heme.
Salt bridge interactions between the Arg 141 and Lys 127 residues of the dimers are broken.
The two αβ dimers rotate some 15° about an imaginary pivot passing through the α‐β subunits.
c. Blue Dextran, Vitamin B-12 and Cytochrome c
a. Cytochrome c, Vitamin B-12, Blue Dextran
e. Blue Dextran, Cytochrome c and Vitamin B-12
d. Cytochrome c, Blue Dextran, Vitamin B-12
b. Vitamin B-12, Cytochrome c and Blue Dextran
Removing urea by dialysis and then allowing air oxidation of the denatured protein restored the protein to its original functionality.
Denaturing the protein with both urea and β-mercaptoethanol yielded an inactive protein.
Protein folding is determined by its primary sequence.
Exposing the denatured protein to air oxidation and then dialysis to remove urea restored the protein to its original functionality.
shape remodeling and then chemical oxidation
chemical reduction and then shape remodeling
chemical reduction and then chemical oxidation
chemical oxidation and then shape remodeling
shape remodeling and then chemical reduction
The two αβ dimers rotate some 15° about an imaginary pivot passing through the α-β subunits.
the lysine residues are neutral, which eliminates electrostatic repulsion between the R groups.
the lysine side chain do not change configuration with pH.
the lysine residues are negatively charged, which electrostatically stabilizes the helix.
the positive charges on the lysine residues stabilizes the α-helix.
the high concentration of OH− ions in solution reduces the electrostatic repulsion between the R-groups.
Antigenic determinants reside only in the variable region of the light chains.
Fetal hemoglobin has S instead of H at position 143 leading to two fewer positive charges in the BPG binding cavity.
Fetal hemoglobin has a higher affinity for oxygen than does maternal hemoglobin because it has a higher affinity for the allosteric regulator 2,3-bisphosphoglycerate.
The immunoglobulin domain is a stable scaffold containing two antiparallel β-sheets upon which to display hypervariable loops.
If an aspartic acid residue were present in the interior of a globular protein, it would most likely be deprotonated and thus negatively charged.
Parallel β-sheets characteristically distribute hydrophobic side chains on both sides of the sheet, and antiparallel β-sheets are usually arranged with all their hydrophobic residues on one side of the sheet.
Silk fibers consist of fibroin proteins consisting of alternating A and G or S residues.
Planarity of the peptide bond means that no rotation occurs about the N-Cα bond while rotation is allowed about the C(O)-N and Cα-C(O) bonds.
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