Literature DB >> 2790052

Hemoglobin Nouakchott [alpha 114(GH2)Pro----Leu]: a new hemoglobin variant displaying an unusual increase in hydrophobicity.

H Wajcman1, J Delaunay, A Francina, J Rosa, F Galacteros.   

Abstract

The most striking fact in Hb Nouakchott [alpha 114(GH2)Pro----Leu] is the highly increased hydrophobicity of the abnormal chain. In comparison to other variants carrying the same amino-acid substitution, but at another position, the involvement of the environmental domains in the expression of the hydrophobicity is shown. Even though the substitution concerned a proline residue, it was without consequences on the oxygen binding and the stability of the molecule.

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Year:  1989        PMID： 2790052     DOI： 10.1016/0167-4838(89)90114-3

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN： 0006-3002


  3 in total

1.  Separation of adult chains of abnormal haemoglobin: Identification by reversed-phase high-performance liquid chromatography.

Authors:  Paul Angoué Yapo; Jacques Y Datté; Ayekoé Yapo; Henri Wachman
Journal:  J Clin Lab Anal       Date:  2004       Impact factor: 2.352

2.  Familial secondary erythrocytosis due to increased oxygen affinity is caused by destabilization of the T state of hemoglobin Brigham (α₂β₂(Pro100Leu)).

Authors:  Todd L Mollan; Bindu Abraham; Michael Brad Strader; Yiping Jia; Jay N Lozier; John S Olson; Abdu I Alayash
Journal:  Protein Sci       Date:  2012-08-21       Impact factor: 6.725

3.  Structural basis for the antipolymer activity of Hb ζ2βs2 trapped in a tense conformation.

Authors:  Martin K Safo; Tzu-Ping Ko; Eric R Schreiter; J Eric Russell
Journal:  J Mol Struct       Date:  2015-11-05       Impact factor: 3.196
  3 in total

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