Proton nuclear magnetic resonance studies of hemoglobin providence (β82EF6 Lys → Asn or Asp): a residue involved in anion binding

High-resolution proton nuclear magnetic resonance studies of hemoglobins Providence-Asn (beta82EF6 Lys replaced by Asn) and Providence-Asp (beta82EF6 Lys replaced by Asp) show that different amino acid substitutions at the same position in the hemoglobin molecule have different effects on the struct...

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Veröffentlicht in:	Biochemistry (Easton) 1978-03, Vol.17 (5), p.791-795
Hauptverfasser:	Wiechelman, Karen J, Fox, Jack, McCurdy, Paul R, Ho, Chien
Format:	Artikel
Sprache:	eng
Schlagworte:	Adult Anions Binding Sites Carboxyhemoglobin Chlorides - pharmacology Diphosphoglyceric Acids - pharmacology Female Hemoglobins, Abnormal Humans Magnetic Resonance Spectroscopy Phytic Acid - pharmacology Protein Conformation - drug effects Structure-Activity Relationship
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