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Volumn 294, Issue 2, 2001, Pages 95-101

Use of surface plasmon resonance for real-time measurements of the global conformational transition in human phenylalanine hydroxylase in response to substrate binding and catalytic activation

Author keywords

Affinity; Association and dissociation rate; Biacore; Binding; Biosensor; Phenylalanine hydroxylase; Surface plasmon resonance

Indexed keywords

AMINO ACIDS; BIOSENSORS; DISSOCIATION; ENZYMES; PLASMONS; RESONANCE; TIME MEASUREMENT;

EID: 0035879403     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1006/abio.2001.5163     Document Type: Article
Times cited : (38)

References (24)
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    • A comparison of kinetic and regulatory properties of the tetrameric and dimeric forms of wild-type and Thr427Pro mutant human phenylalanine hydroxylase. Contribution of the flexible hinge region Asp425-Gln429 to the tetramerization and cooperative substrate binding
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  • 16
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    • Karlsson, R.1    St Åhlberg, R.2
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    • High-resolution multiwavelength surface plasmon resonance spectroscopy for probing conformational and electronic changes in redox proteins
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    • Boussaad, S.1    Pean, J.2    Tao, N.J.3
  • 24
    • 0033771865 scopus 로고    scopus 로고
    • Microheterogeneity of recombinant human phenylalanine hydroxylase as a result of nonenzymatic deamidations of labile amide containing amino acids. Effects on catalytic and stability properties
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6302-6310
    • Solstad, T.1    Flatmark, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.