Equilibrium unfolding studies of monellin: The double-chain variant appears to be more stable than the single-chain variant

Biochemistry

Volumn 50, Issue 13, 2011, Pages 2434-2444

  Aghera, Nilesh ^a   Earanna, Ninganna ^b   Udgaonkar, Jayant B ^a  

^a TATA INSTITUTE OF FUNDAMENTAL RESEARCH   (India)

^b UNIVERSITY OF AGRICULTURAL SCIENCES   (India)

Author keywords

[No Author keywords available]

Indexed keywords

DOUBLE CHAIN; EQUILIBRIUM BINDING; EXPONENTIAL DEPENDENCE; GUANIDINE HYDROCHLORIDE; KINETIC STABILITY; NATIVE STATE; NATURALLY OCCURRING; PROTEIN CONCENTRATIONS; PROTEIN STABILITY; PROTEIN VARIANTS; RESIDUAL STRUCTURE; SIDE CHAINS; STABILIZING INTERACTIONS; SWEET PROTEIN; THERMODYNAMIC COUPLING; TWO-STATE;

CARBOXYLATION; COMPLEXATION; CONCENTRATION (PROCESS); FREE ENERGY;

PROTEINS;

CARBOXYLIC ACID; GUANIDINE; MONELLIN; PROTEIN;

ARTICLE; BINDING AFFINITY; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; CROSS COUPLING REACTION; DISSOCIATION; ENERGY CONVERSION; EQUILIBRIUM CONSTANT; KINETICS; PH; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; STRAIN DIFFERENCE; THERMODYNAMICS;

CIRCULAR DICHROISM; DIMERIZATION; GUANIDINE; HYDROGEN-ION CONCENTRATION; KINETICS; MODELS, MOLECULAR; OSMOLAR CONCENTRATION; PLANT PROTEINS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN STABILITY; PROTEIN UNFOLDING; RECOMBINANT PROTEINS; SPECTROMETRY, FLUORESCENCE;

EID: 79953228858     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi101955f     Document Type: Article

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