A small molecule chemical chaperone optimizes its unfolded state contraction and denaturant like properties

Scientific Reports

Volumn 3, Issue , 2013, Pages

  Sharma, Sunny ^a   Sarkar, Suparna ^a   Paul, Simanta Sarani ^a   Roy, Syamal ^a   Chattopadhyay, Krishnananda ^a  

^a INDIAN INSTITUTE OF CHEMICAL BIOLOGY   (India)

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; CHAPERONE; KINETOPLASTID MEMBRANE PROTEIN 11, LEISHMANIA DONOVANI; LEISHMANIA VACCINE; MEMBRANE PROTEIN; MUTANT PROTEIN; PROTOZOAL PROTEIN; SUCROSE; TRYPTOPHAN;

ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; IMMUNOLOGY; LEISHMANIA; LEISHMANIASIS; METABOLISM; MUTATION; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN UNFOLDING;

ARGININE; LEISHMANIA; LEISHMANIASIS; LEISHMANIASIS VACCINES; MEMBRANE GLYCOPROTEINS; MODELS, MOLECULAR; MOLECULAR CHAPERONES; MUTANT PROTEINS; MUTATION; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN UNFOLDING; PROTOZOAN PROTEINS; SUCROSE; TRYPTOPHAN;

EID: 84890728539     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep03525     Document Type: Article

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