Title : A chemometric analysis of ligand-induced changes in intrinsic fluorescence of folate binding protein indicates a link between altered conformational structure and physico-chemical characteristics.

Pub. Date : 2009 Dec

PMID : 20030974






4 Functional Relationships(s)
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1 For the purpose of achieving further information we analyzed ligand (folate and methotrexate)-induced changes in the fluorescence landscape of FBP. Folic Acid folate receptor alpha Bos taurus
2 The sharp decrease in hydrophobicity at pI=7-8 following binding of folate accords fairly well with the disappearance of strongly hydrophobic tryptophan residues from the solvent-exposed surface of FBP. Folic Acid folate receptor alpha Bos taurus
3 The PARAFAC has thus proven useful to establish a hitherto unexplained link between parallel changes in conformational structure and physico-chemical characteristics of FBP induced by folate binding. Folic Acid folate receptor alpha Bos taurus
4 This could suggest a rapid and firm complexation of folate to FBP, blocking access of competing ligands. Folic Acid folate receptor alpha Bos taurus