Confinement in nanopores can destabilize α-helix folding proteins and stabilize the β structures

Journal of Chemical Physics

Volumn 135, Issue 12, 2011, Pages

  Javidpour, Leili ^a   Sahimi, Muhammad ^b  

^a INSTITUTE FOR STUDIES IN THEORETICAL PHYSICS AND MATHEMATICS IPM   (Iran)

^b University of Southern California   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL CELLS; CHAPERONIN; CONFINED ENVIRONMENT; CONFINED PORES; CONFINING WALLS; CONFORMATIONAL TRANSITIONS; CURRENT THEORIES; ENTROPIC EFFECTS; ENZYME STABILIZATION; EXPERIMENTAL OBSERVATION; FOLDED STATE; FOLDING RATES; FREE ENERGY SURFACE; IN-SILICO; IN-VITRO; IN-VIVO; MOLECULAR DYNAMICS SIMULATIONS; NATIVE STATE; PARKINSONS DISEASE; PROTEIN STABILITY; THEORETICAL EXPLANATION;

ENTROPY; FREE ENERGY; MOLECULAR DYNAMICS; NANOPORES; PORE SIZE; PROTEIN FOLDING;

PROTEINS;

PROTEIN;

ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; MOLECULAR DYNAMICS; NANOPORE; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE;

MODELS, MOLECULAR; MOLECULAR DYNAMICS SIMULATION; NANOPORES; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEINS;

EID: 80053512774     PISSN: 00219606     EISSN: None     Source Type: Journal    
DOI: 10.1063/1.3641482     Document Type: Article

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