Properties of normal and mutant polypeptide fragments from the dimer self-association sites of human red cell spectrin

European Biophysics Journal

Volumn 28, Issue 3, 1999, Pages 208-215

  Lecomte, M C ^a   Nicolas, G ^a   Dhermy, D ^a   Pinder, J C ^b   Gratzer, W B ^b  

^a INSERM   (France)

^b KING'S COLLEGE LONDON   (United Kingdom)

Author keywords

Erythrocyte; Hereditary elliptocytosis; Self association; Spectrin

Indexed keywords

ALANINE; ARGININE; DIMER; MUTANT PROTEIN; POLYPEPTIDE; SPECTRIN; TRYPTOPHAN; VALINE;

ALPHA HELIX; AMINO ACID SUBSTITUTION; ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; DISEASE SEVERITY; DISSOCIATION; ERYTHROCYTE; HEREDITARY ELLIPTOCYTOSIS; HUMAN; HUMAN CELL; PROTEIN ASSEMBLY; PROTEIN CONFORMATION; PROTEIN DENATURATION; SEDIMENTATION RATE;

BINDING SITES; BIOPHYSICS; CIRCULAR DICHROISM; DIMERIZATION; ERYTHROCYTES; HUMANS; MUTAGENESIS, SITE-DIRECTED; PEPTIDE FRAGMENTS; POINT MUTATION; PROTEIN CONFORMATION; SPECTRIN;

EID: 0032960680     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002490050201     Document Type: Article

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