Conformational states of HRPA1 induced by thermal unfolding: Effect of low molecular weight solutes

Biopolymers

Volumn 75, Issue 2, 2004, Pages 173-186

  Carvalho, Ana Sofia L ^a   Santos, Andrea M ^a   Neves Petersen, Maria Teresa ^b   Petersen, Steffen B ^b   Aires Barros, Maria Raquel ^a   Pinho E Melo, Eduardo ^a,c  

^a INSTITUTO SUPERIOR TÉCNICO   (Portugal)

^b AALBORG UNIVERSITY   (Denmark)

^c UNIVERSITY OF ALGARVE   (Portugal)

Author keywords

Acrylamide quenching; CD; Fluorescence resonance energy transfer; Heme; Horseradish peroxidase A1; Low molecular weight solutes; Peroxidase calcium ions; Tryptophan fluorescence lifetimes; Unfolding intermediate state; Unfolding pathway

Indexed keywords

CALCIUM; ENERGY TRANSFER; ENZYMES; FLUORESCENCE; MOLECULAR WEIGHT; QUENCHING;

CONFORMATIONAL STATES; FLUOROPHORES; THERMAL UNFOLDING;

THERMOANALYSIS;

CALCIUM ION; HORSERADISH PEROXIDASE; MELEZITOSE; SORBITOL; TREHALOSE; UNCLASSIFIED DRUG;

ARTICLE; CIRCULAR DICHROISM; DENATURATION; ENERGY TRANSFER; FLUORESCENCE; PROTEIN CONFORMATION; PROTEIN DEPLETION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; QUANTUM YIELD; SOLUTE; THERMAL EXPOSURE;

BACTERIAL OUTER MEMBRANE PROTEINS; CIRCULAR DICHROISM; FLUORESCENCE RESONANCE ENERGY TRANSFER; HEAT; PROTEIN CONFORMATION; PROTEIN DENATURATION; SPECTROMETRY, FLUORESCENCE; TIME FACTORS; TRYPTOPHAN;

ARMORACIA RUSTICANA;

EID: 4944228100     PISSN: 00063525     EISSN: None     Source Type: Journal    
DOI: 10.1002/bip.20100     Document Type: Article

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