NMR investigations on residue level unfolding thermodynamics in DLC8 dimer by temperature dependent native state hydrogen exchange

Journal of Biomolecular NMR

Volumn 44, Issue 1, 2009, Pages 1-11

  Mohan, P M Krishna ^a   Chakraborty, Swagata ^a   Hosur, Ramakrishna V ^a  

^a TATA INSTITUTE OF FUNDAMENTAL RESEARCH   (India)

Author keywords

Dynein light chain protein; Native state hydrogen exchange; Nuclear magnetic resonance; Thermal stability; Unfolding energetics

Indexed keywords

DIMER; DYNEIN LIGHT CHAIN PROTEIN 8; HYDROGEN; PROTEIN DLC8; UNCLASSIFIED DRUG;

ARTICLE; CALORIMETRY; DENATURATION; HIGH TEMPERATURE; ION EXCHANGE; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FOLDING; PROTEIN PURIFICATION; PROTEIN STRUCTURE; THERMODYNAMICS; THERMOSTABILITY;

ALGORITHMS; DYNEIN ATPASE; HYDROGEN; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN MULTIMERIZATION; TEMPERATURE; THERMODYNAMICS;

EID: 63649135856     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-009-9311-5     Document Type: Article

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