Probing the conformation of hemoglobin presbyterian in the R-state

• Published in: Journal of Protein Chemistry Vol. 22; no. 3; pp. 221 - 230
• Main Authors: Acharya, Seetharama A, Malavalli, Ashok, Peterson, Eric, Sun, Philip D, Ho, Chien, Prabhakaran, Muthuchidambaram, Arnone, Arthur, Manjula, Belur N, Friedman, Joel M
• Format: Journal Article
• Language: English
• Published: United States Springer Nature B.V 01.04.2003
• Subjects: Affinity; Allosteric properties; Allosteric Regulation; Allosteric Site; Animals; Animals, Genetically Modified; Binding sites; Effectors; Hemoglobin; Hemoglobin A - chemistry; Hemoglobin A - metabolism; Hemoglobins, Abnormal - chemistry; Hemoglobins, Abnormal - genetics; Hemoglobins, Abnormal - metabolism; Humans; Inositols; Ions - chemistry; Kinetics; Ligands; Magnetic Resonance Spectroscopy; Magnetic studies; Microenvironments; Models, Molecular; Molecular biology; Molecular modelling; Mutation; NMR; Nuclear magnetic resonance; Oxygen; Oxygen - chemistry; Oxygen - metabolism; Photochemistry; Protein Structure, Quaternary; Proteins; Signatures; Spectrum Analysis, Raman; Swine; Temperature

The influence of allosteric effectors on the R-state (liganded) conformation of Tg-HbP (human hemoglobin Presbyterian expressed in transgenic pig) has been probed using a number of biophysical techniques, and the results have been compared with that of liganded of HbA (human normal adult hemoglobin)...