Protein folding and stability investigated by fluorescence, circular dichroism (CD), and nuclear magnetic resonance (NMR) spectroscopy: The flavodoxin story

Journal of Biotechnology

Volumn 79, Issue 3, 2000, Pages 281-298

  Van Mierlo, Carlo P M ^a   Steensma, Elles ^b  

^a WAGENINGEN UNIVERSITY   (Netherlands)

^b UPPSALA UNIVERSITY   (Sweden)

Author keywords

Circular dichroism; Co operative and non co operative transition; Equilibrium unfolding; Flavodoxin; Fluorescence; NMR; Three state model

Indexed keywords

APOFLAVODOXIN; APOPROTEIN; BACTERIAL PROTEIN; CUTINASE; FLAVINE MONONUCLEOTIDE; FLAVODOXIN; HYDROGEN; UNCLASSIFIED DRUG;

ANABAENA; ANALYTIC METHOD; AZOTOBACTER VINELANDII; CIRCULAR DICHROISM; CONFERENCE PAPER; CONFORMATIONAL TRANSITION; FLUORESCENCE SPECTROSCOPY; MODEL; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STABILITY; TECHNIQUE;

AMIDES; CIRCULAR DICHROISM; FLAVODOXIN; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTONS; SPECTROMETRY, FLUORESCENCE;

AZOTOBACTER VINELANDII;

EID: 0034717064     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-1656(00)00244-3     Document Type: Conference Paper

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