Effects of beta 6 amino acid hydrophobicity on stability and solubility of hemoglobin tetramers.

Abstract:

:The relationship between different amino acids at the beta 6 position of hemoglobin and tetramer stability was addressed by a site-directed mutagenesis approach. Precipitation rates during mechanical agitation of oxyhemoglobins with Gln, Ala, Val, Leu and Trp at the beta 6 position increased 2, 5, 13, 21 and 53 times, respectively, compared with that for Hb A. There was a linear relationship between the log of the precipitation rate constant and amino acid hydrophobicity at the beta 6 position, suggesting that enhanced precipitation of oxy Hb S during mechanical agitation results in part from increased hydrophobicity of beta 6 Val. Deoxyhemoglobin solubility increased in the order of beta 6 Ile, Leu, Val, Trp, Gln, Ala and Glu suggesting that hydrophobic interactions between beta 6 Val and the acceptor site of another hemoglobin molecule during deoxy-Hb S polymerization not only depend on hydrophobicity but also on stereospecificity of the amino acid side chain at the beta 6 position. Furthermore, our results indicate that hydrophobic amino acids at the beta 6 position which promote tetramer instability in the oxy form do not necessarily promote polymerization in the deoxy form.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Adachi K,Kim JY,Konitzer P,Asakura T,Saviola B,Surrey S

doi

10.1016/0014-5793(93)81130-r

subject

Has Abstract

pub_date

1993-01-02 00:00:00

pages

47-50

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(93)81130-R

journal_volume

315

pub_type

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