Chapter 5
Amino acids in this category, which includes histidine and aspartic acid, have side chains capable of accepting or donating a proton.
What are charged polar amino acids?
A secondary structure characterized by perpendicular hydrogen bonding between adjacent parallel or antiparallel strands.
What is a ß sheet?
This, specific, myosin type is involved in muscle contraction.
What is myosin II?
Ammonia is converted into this, less toxic, molecule in the liver, requiring the hydrolysis of three molecules of ATP.
What is urea?
Amino acids in this category, which includes tryptophan, have side chains characterized by rings with conjugated systems of delocalized electrons.
What are nonpolar aromatic amino acids?
A secondary structure characterized by tight coils and acute negative φ and ψ angles (−70° to −60° and −50° to −40° respectively).
What is an α helix?
The binding of this molecule to an allosteric site on hemoglobin stabilizes the T-state and decreases O2 affinity.
What is 2,3-bisphosphoglycerate (2,3-BPG)?
Carbamoyl phosphate and ornithine combine to make citrulline in this part of a liver cell.
What is a mitochondrion?
A planar bond caused by the delocalization of electrons by resonance in the backbone of a polypeptide.
What is an amide bond (peptide bond)?
An angle that describes the rotation about the Namide—Cα bond.
What is the φ angle?
An immunoglobulin fragment composed only from the constant regions of two immunoglobulin heavy chains responsible for the activation of complement or other effectors.
What is the fragment crystallizable region (Fc)?
This enzyme catalyzes the dehydration synthesis of glutamate and ammonium to glutamine coupled to ATP hydrolysis.
What is glutamine synthetase?
Amino acids in this category, which includes glutamine, are characterized by having electronegative atoms in their side chains that do not readily ionize.
What are polar uncharged amino acids?
What is α-keratin?
A phenomenon where salt bridges are formed between and within the α-globin and ß-globin subunits of hemoglobin due to the protonation of residues at lower pH.
What is the Bohr effect?
This enzyme performs the reductive amination of α-ketoglutarate to glutamate.
What is glutamate dehydrogenase?
This amino acid has an imino group that restricts rotation about φ.
What is proline?
A triple helical protein that is the most abundant protein in vertebrates.
What is collagen?
This immunoglobulin pentamer is produced by short-lived plasma cells in the early stages of the immune response.
What is immunoglobulin M (IgM)?
Pyridoxal phosphate (PLP), the active form of this vitamin, is a cofactor in the transamination of an amino acid and an α-keto acid.
What is vitamin B6 (pyridoxine)?