Isolation, purification and 13C- and 1H-n.m.r. assignments of peptide [1-24] of human serum albumin.
Isolation, purification and 360 MHz 1H- and 13C-n.m.r. spectra of the residue corresponding to the NH2-terminal peptide fragment [1-24] of human serum albumin are reported. The various resonances have been assigned to individual amino acid residues and their spatial microenvironment has been determined in a straightforward manner on the basis of (i) pH dependent chemical shifts; (ii) combined use of multiple and selective proton-decoupled 1H- and 13C-n.m.r. spectra; (iii) the characteristic pK values exhibited by protons adjacent to sites of ionization in the molecule; and (iv) comparison of the spectra with the NH2-terminal tripeptide segment of human albumin. The pK values of different ionizable groups all fall in the normal range expected for each titrating sites and support a model of peptide fragment [1-24] in which there is no special structure-forming strong associations. These results are in agreement with those obtained by CD spectroscopy.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D002942:Circular Dichroism; D006801:Humans; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D010446:Peptide Fragments / Q000302:isolation & purification*; D011487:Protein Conformation; D012709:Serum Albumin / Q000302:isolation & purification*; D000075462:Serum Albumin, Human
D000596:Amino Acids; D010446:Peptide Fragments; D012709:Serum Albumin; C042510:serum albumin (1-24); D000075462:Serum Albumin, Human