Absolute free energy and entropy of a mobile loop of the enzyme acetylcholinesterase

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Absolute free energy and entropy of a mobile loop of the enzyme acetylcholinesterase is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1021/JP900308Y
P932PMC publication ID2747743
P698PubMed publication ID19435302
P5875ResearchGate publication ID24420748

P2093author name stringHagai Meirovitch
Mihail Mihailescu
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Structure of acetylcholinesterase complexed with the nootropic alkaloid, (-)-huperzine AQ27734318
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Computer simulation of the free energy of peptides with the local states method: analogues of gonadotropin releasing hormone in the random coil and stable statesQ40685170
Free volume hypothetical scanning molecular dynamics method for the absolute free energy of liquidsQ41497542
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Entropy and free energy of a mobile protein loop in explicit waterQ42140475
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Conformational energy landscape of the acyl pocket loop in acetylcholinesterase: a Monte Carlo-generalized Born model studyQ45069351
Evaluating the Accuracy of the Quasiharmonic ApproximationQ46144156
Modeling loop reorganization free energies of acetylcholinesterase: a comparison of explicit and implicit solvent models.Q51986757
Recording spectrophotometric method for determination of dissociation and phosphorylation constants for the inhibition of acetylcholinesterase by organophosphates in the presence of substrateQ52481665
Acetylcholinesterase.Q52887410
Engineering resistance to 'aging' of phosphylated human acetylcholinesterase. Role of hydrogen bond network in the active center.Q54226185
Stability of polypeptide conformational states. II. Folding of a polypeptide chain by the scanning simulation method, and calculation of the free energy of the statistical coilQ68020418
Stability of polypeptide conformational states as determined by computer simulation of the free energyQ69052607
Multiple conformational states of proteins: a molecular dynamics analysis of myoglobinQ69706390
Kinetics for the inhibition of acetylcholinesterase from the electric eel by some organophosphates and carbamatesQ71296767
Affinity and phosphorylat1on constants of a series of O,O-dialkyl malaoxons and paraoxons with acetylcholinesteraseQ71340137
Computer simulation of the free energy of polymer chains with excluded volume and with finite interactionsQ77819303
Packing structures and transitions in liquids and solidsQ81031838
Stability of the Free and Bound Microstates of a Mobile Loop of α-Amylase Obtained from the Absolute Entropy and Free EnergyQ86831965
P433issue22
P407language of work or nameEnglishQ1860
P304page(s)7950-7964
P577publication date2009-06-01
P1433published inJournal of Physical Chemistry BQ668669
P1476titleAbsolute free energy and entropy of a mobile loop of the enzyme acetylcholinesterase
P478volume113

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cites work (P2860)
Q28385662Absolute free energy of binding of avidin/biotin, revisited
Q41870856Assessing protein loop flexibility by hierarchical Monte Carlo sampling
Q28396455Calculation of the Absolute Free Energy of Binding and Related Entropies with the HSMD-TI Method: The FKBP12-L8 Complex
Q42180577Entropy and Free Energy of a Mobile Loop Based on the Crystal Structures of the Free and Bound Proteins
Q41912526New method for calculating the absolute free energy of binding: the effect of a mobile loop on the avidin/biotin complex
Q42593384Relative stability of the open and closed conformations of the active site loop of streptavidin

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