Dimer-monomer equilibrium of human thymidylate synthase monitored by fluorescence resonance energy transfer

Protein Science

Volumn 19, Issue 5, 2010, Pages 1023-1030

  Genovese, Filippo ^a   Ferrari, Stefania ^a   Guaitoli, Giambattista ^a   Caselli, Monica ^a   Costi, M Paola ^a   Ponterini, Glauco ^a  

^a UNIVERSITY OF MODENA AND REGGIO EMILIA   (Italy)

Author keywords

Active site masking; Dimer monomer equilibrium; Fluorescent probes; FRET; Human thymidylate synthase; Oligomeric proteins

Indexed keywords

CYSTEINE; MONOMER; THYMIDYLATE SYNTHASE;

ABSORPTION SPECTROSCOPY; ARTICLE; DIMERIZATION; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME STRUCTURE; FLUORESCENCE RESONANCE ENERGY TRANSFER; PRIORITY JOURNAL;

ALLOSTERIC SITE; CATALYTIC DOMAIN; FLUORESCENCE RESONANCE ENERGY TRANSFER; HUMANS; KINETICS; MODELS, MOLECULAR; PROTEIN MULTIMERIZATION; THYMIDYLATE SYNTHASE;

EID: 77951528478     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.379     Document Type: Article

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