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Volumn 39, Issue 36, 2000, Pages 11154-11162

Difference in the mechanisms of the cold and heat induced unfolding of thioredoxin h from Chlamydomonas reinhardtii: Spectroscopic and calorimetric studies

(4) Richardson III, J M a Lemaire, S D b,c Jacquot, J P c,d Makhatadze, G I a

a PENN STATE COLLEGE OF MEDICINE (United States)

b INSTITUTE OF PLANT SCIENCES PARIS SACLAY IPS2 (France)

c UNIVERSITY OF GENEVA (Switzerland)

d UNIVERSITÉ DE LORRAINE (France)

Author keywords

[No Author keywords available]

Indexed keywords

THIOREDOXIN;

ARTICLE; CHLAMYDOMONAS REINHARDTII; CHLOROPLAST; CIRCULAR DICHROISM; DIFFERENTIAL SCANNING CALORIMETRY; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY; SPECTROSCOPY; THERMODYNAMICS;

ANIMALS; CALORIMETRY, DIFFERENTIAL SCANNING; CHLAMYDOMONAS REINHARDTII; CIRCULAR DICHROISM; COLD; GLYCINE; HEAT; HYDROCHLORIC ACID; HYDROGEN-ION CONCENTRATION; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SPECTROMETRY, FLUORESCENCE; THERMODYNAMICS; THIOREDOXIN;

BACTERIA (MICROORGANISMS); CHLAMYDOMONAS REINHARDTII;

EID: 0034641693 PISSN: 00062960 EISSN: None Source Type: Journal
DOI: 10.1021/bi000610b Document Type: Article

Times cited : (38)

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