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Volumn 40, Issue 13, 2001, Pages 3974-3984
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Free energies of urea and of thermal unfolding show that two tandem repeats of spectrin are thermodynamically more stable than a single repeat
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Author keywords
[No Author keywords available]
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Indexed keywords
THERMAL UNFOLDING;
ADDITION REACTIONS;
CRYSTAL STRUCTURE;
FREE ENERGY;
THERMODYNAMIC STABILITY;
UREA;
X RAY CRYSTALLOGRAPHY;
PROTEINS;
CYTOSKELETON PROTEIN;
FODRIN;
UREA;
ANIMAL TISSUE;
ARTICLE;
CRYSTAL STRUCTURE;
DENATURATION;
ENERGY TRANSFER;
MOLECULAR CLONING;
MOLECULAR STABILITY;
NONHUMAN;
PRIORITY JOURNAL;
TANDEM REPEAT;
THERMAL ANALYSIS;
THERMODYNAMICS;
AMINO ACID MOTIFS;
ANIMALS;
CHICKENS;
CIRCULAR DICHROISM;
MODELS, CHEMICAL;
MUTAGENESIS, SITE-DIRECTED;
PEPTIDE FRAGMENTS;
PROTEIN DENATURATION;
PROTEIN FOLDING;
PROTEIN STRUCTURE, SECONDARY;
REPETITIVE SEQUENCES, AMINO ACID;
SPECTRIN;
SPECTROMETRY, FLUORESCENCE;
TEMPERATURE;
THERMODYNAMICS;
TRYPTOPHAN;
UREA;
ANIMALIA;
GALLUS GALLUS;
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EID: 0035799317
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi0025159 Document Type: Article |
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Times cited : (48)
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References (52)
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