Surface and interface beta-chain residues synergistically affect hemoglobin assembly.

doi:10.1006/bbrc.2000.2504

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Article

Surface and interface beta-chain residues synergistically affect hemoglobin assembly.

Biochemical and biophysical research communications - 21 Apr 2000

Yamaguchi T, Yang Y, McDonald M J, Adachi K

Abstract excerpt

Homo- and heterotetramer formations of beta112 variants (beta(112Cys-->Asp), beta(112Cys-->Ser), beta(112Cys-->Thr), and beta(112Cys-->Val)) of hemoglobin were characterized in the presence and absence of beta(16Gly-->Asp) in vitro. In all cases an alteration in overall surface charge (beta(16Gly...

Topics

Amino Acid Substitution
Genetic Variation
Globins
Hemoglobins
Humans
Kinetics
Macromolecular Substances
Mutagenesis, Site-Directed
Protein Structure, Quaternary
Recombinant Proteins
Static Electricity

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