Hemoglobin Einstein

Semisynthetic deletion in the B-helix of the α-chain

Sonati Srinivasulu, Belur N. Manjula, Ronald L. Nagel, Ching Hsuan Tsai, Chien Ho, Muthuchidambaran Prabhakaran, Seetharama A. Acharya

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

The influence of the deletion of the tetra peptide segment α 23-26 of the B-helix of the ot-chain of hemoglobin-A on its assembly, structure, and functional properties has been investigated. The hemoglobin with the deletion, ss-Hemoglobin-Einstein, is readily assembled from semisynthetic α1-141des23-26 globin and human βA-chain. The deletion of α23-26 modulates the O2 affinity of hemoglobin in a buffer/allosteric effector specific fashion, but has little influence on the Bohr effect. The deletion has no influence on the thermodynamic stability of the α1β 1 and the α1β2 interface. The semisynthetic hemoglobin exhibits normal intersubunit interactions at the α1β1 and α1β2 interfaces as reflected by 1H-NMR spectroscopy. Molecular modeling studies of ss-Hemoglobin-Einstein suggest that the segment α 28-35 is in a helical conformation, while the segment α 19-22 is the nonhelical AB region. The shortened B-helix conserves the interactions of α1β1 interface. The results demonstrate a high degree of plasticity in the hemoglobin structure that accommodates the deletion of α23-26 without perturbing its overall global conformation.

Original languageEnglish (US)
Pages (from-to)1266-1275
Number of pages10
JournalProtein Science
Volume13
Issue number5
DOIs
StatePublished - May 2004

Fingerprint

Hemoglobins
Conformations
Molecular modeling
Globins
Thermodynamics
Nuclear magnetic resonance spectroscopy
Plasticity
Buffers
Thermodynamic stability
Magnetic Resonance Spectroscopy
hemoglobin Einstein
Peptides

Keywords

  • H-NMR spectroscopy
  • Molecular modeling
  • Oxygen affinity
  • Shortened B-helix
  • Stuctural plasticity
  • Subunit interfaces
  • Thermodynamic stability

ASJC Scopus subject areas

  • Biochemistry

Cite this

Srinivasulu, S., Manjula, B. N., Nagel, R. L., Tsai, C. H., Ho, C., Prabhakaran, M., & Acharya, S. A. (2004). Hemoglobin Einstein: Semisynthetic deletion in the B-helix of the α-chain. Protein Science, 13(5), 1266-1275. https://doi.org/10.1110/ps.03567804

Hemoglobin Einstein : Semisynthetic deletion in the B-helix of the α-chain. / Srinivasulu, Sonati; Manjula, Belur N.; Nagel, Ronald L.; Tsai, Ching Hsuan; Ho, Chien; Prabhakaran, Muthuchidambaran; Acharya, Seetharama A.

In: Protein Science, Vol. 13, No. 5, 05.2004, p. 1266-1275.

Research output: Contribution to journalArticle

Srinivasulu, S, Manjula, BN, Nagel, RL, Tsai, CH, Ho, C, Prabhakaran, M & Acharya, SA 2004, 'Hemoglobin Einstein: Semisynthetic deletion in the B-helix of the α-chain', Protein Science, vol. 13, no. 5, pp. 1266-1275. https://doi.org/10.1110/ps.03567804
Srinivasulu S, Manjula BN, Nagel RL, Tsai CH, Ho C, Prabhakaran M et al. Hemoglobin Einstein: Semisynthetic deletion in the B-helix of the α-chain. Protein Science. 2004 May;13(5):1266-1275. https://doi.org/10.1110/ps.03567804
Srinivasulu, Sonati ; Manjula, Belur N. ; Nagel, Ronald L. ; Tsai, Ching Hsuan ; Ho, Chien ; Prabhakaran, Muthuchidambaran ; Acharya, Seetharama A. / Hemoglobin Einstein : Semisynthetic deletion in the B-helix of the α-chain. In: Protein Science. 2004 ; Vol. 13, No. 5. pp. 1266-1275.
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