Chaperone-like activity of α-cyclodextrin via hydrophobic nanocavity to protect native structure of ADH

Carbohydrate Research

Volumn 345, Issue 2, 2010, Pages 243-249

  Barzegar, Abolfazl ^a,b   Moosavi Movahedi, Ali A ^b   Mahnam, Karim ^b   Ashtiani, Saman Hosseini ^b  

^a UNIVERSITY OF TABRIZ   (Iran)

^b UNIVERSITY OF TEHRAN   (Iran)

Author keywords

Cyclodextrin; Aggregation; Blind docking; Hydrophobic nanocavity; Microenvironment; Molecular dynamic simulations

Indexed keywords

ALCOHOL DEHYDROGENASE; ARTIFICIAL CHAPERONE; CHAPERONE ACTION; CHAPERONE-LIKE ACTIVITY; COMPUTATIONAL CALCULATIONS; COMPUTATIONAL TECHNIQUE; DELOCALIZATIONS; HIGH AFFINITY; INCLUSION COMPLEX; MICROENVIRONMENT; MICROENVIRONMENTS; MOLECULAR COMPLEXES; MOLECULAR DYNAMIC SIMULATIONS; NANO-CAVITIES; NATIVE STRUCTURES; PHENYL RINGS; SOLUBILITY ENHANCEMENT; TWO CHAINS;

AMINO ACIDS; COMPUTER SIMULATION; DOCKING; DYNAMIC LIGHT SCATTERING; ENZYME INHIBITION; ENZYMES; HYDROPHOBICITY; MOLECULAR DYNAMICS;

ENZYME ACTIVITY;

ALCOHOL DEHYDROGENASE; ALPHA CYCLODEXTRIN; CHAPERONE; PHENYLALANINE;

ARTICLE; CHEMICAL STRUCTURE; HYDROPHOBICITY; LIGHT SCATTERING; MOLECULAR DOCKING; MOLECULAR DYNAMICS; POLYMERIZATION; PRIORITY JOURNAL; PROTEIN QUATERNARY STRUCTURE; SIMULATION; ULTRAVIOLET RADIATION;

ALCOHOL DEHYDROGENASE; ALPHA-CYCLODEXTRINS; ANIMALS; DRUG DESIGN; HYDROPHOBICITY; LIGANDS; MOLECULAR CHAPERONES; MOLECULAR DYNAMICS SIMULATION; NANOSTRUCTURES; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY;

EID: 72649083567     PISSN: 00086215     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.carres.2009.11.008     Document Type: Article

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