Legume lectin family, the 'natural mutants of the quaternary state', provide insights into the relationship between protein stability and oligomerization

Biochimica et Biophysica Acta - General Subjects

Volumn 1527, Issue 3, 2001, Pages 102-111

  Srinivas, V R ^a   Reddy, G Bhanuprakash ^a   Ahmad, Nisar ^a   Swaminathan, Chittoor P ^a   Mitra, Nivedita ^a   Surolia, Avadhesha ^a  

^a INDIAN INSTITUTE OF SCIENCE   (India)

Author keywords

DSC; Evolution of lectin oligomerization; Legume lectins; Protein stability; Quaternary structure; Subunit interaction

Indexed keywords

AMINO ACID; DIMER; LECTIN; MONOMER; MUTANT PROTEIN; PROTEIN; TETRAMER;

AMINO ACID SEQUENCE; DIMERIZATION; LEGUME; MOLECULAR EVOLUTION; MOLECULAR MODEL; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; REVIEW;

AMINO ACID SEQUENCE; CALORIMETRY, DIFFERENTIAL SCANNING; DIMERIZATION; FABACEAE; LECTINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PLANT LECTINS; PLANTS, MEDICINAL; PROTEIN DENATURATION; PROTEIN FOLDING; SEQUENCE ALIGNMENT;

EID: 0035882421     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0304-4165(01)00153-2     Document Type: Review

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