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Volumn 8, Issue 2, 1998, Pages 211-217

Electrostatic effects in macromolecules: Fundamental concepts and practical modeling

Author keywords

[No Author keywords available]

Indexed keywords

DIELECTRIC CONSTANT; ELECTRIC FIELD; ELECTRICITY; MACROMOLECULE; MODEL; OXIDATION REDUCTION POTENTIAL; PKA; PRIORITY JOURNAL; REVIEW;

EID: 0032054517     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(98)80041-9     Document Type: Article
Times cited : (287)

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    • Protein control of redox potentials of iron-sulfur proteins
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    • Structural origins of redox potentials in Fe-S proteins - Electrostatic potentials of crystal structures
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    • Calculations of electrostatic energies in photosynthetic reaction centers
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    • Solvation free-energy reaction curves for electron-transfer in aqueous solution - Theory and simulation
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    • Binding of azide to human carbonic anydrase II. The role electrostatic complementarity plays in selecting the preferred resonance structure of azide
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    • Calculations of the electrostatic free-energy contributions to the binding free-energy of sulfonamides to carbonic-anhydrase
    • Madura JD, Nakajima Y, Hamilton RM, Wierzbicki A, Warshel A. Calculations of the electrostatic free-energy contributions to the binding free-energy of sulfonamides to carbonic-anhydrase. Struct Chem. 7:1996;131-138.
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    • Electrostatic control of GTP and GDP binding in the oncoprotein P21(ras)
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    • A fast estimate of electrostatic group contributions to the free energy of protein-inhibitor binding
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    • On the calculation of binding free-energies using continuum methods - Application to MHC class-1 protein - Peptide interactions
    • of special interest. Binding free energies of peptides to proteins are evaluated by the Poisson - Boltzmann method, using the charging cycle introduced in earlier PDLD/S studies [15]; however, current results are still not satisfactory both in terms of the observed trends and absolute values.
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    • Electrostatic contributions to protein - Protein binding affinities: Application to Rap/Raf interaction
    • Muegge I, Schweins T, Warshel A. Electrostatic contributions to protein - protein binding affinities: application to Rap/Raf interaction. Proteins. 30:1998;407-423.
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    • Electrostatic complementarity at protein/protein interfaces
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    • Electrostatic basis of enzyme catalysis
    • G. Náray-Szabó, Warshel A. Dordrecht, The Netherlands: Kluwer Academic Publishers
    • Náray-Szabó G, Fuxreiter M, Warshel A. Electrostatic basis of enzyme catalysis. Náray-Szabó G, Warshel A. Computational Approaches to Biochemical Reactivity. 1997;237-294 Kluwer Academic Publishers, Dordrecht, The Netherlands.
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    • The contribution of electrostatic and van-der-Waals interactions to the stereospecificity of the reaction catalyzed by lactate-dehydrogenase
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    • Computational, pulse-radiolytic, and structural investigations of lysine-136 and its role in the electrostatic triad of human Cu, Zn superoxide dismutase
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    • On the origin of the catalytic power of acetylcholinesterase: Computer simulation studies
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    • Boundary conditions for single-ion diffusion
    • + through the gramicidin channel. This is done by comparing the calculated and observed conductance. It is found that the barriers calculated by the approach of Roux and Karplus [76] drastically overestimate the actual barrier whereas the profile obtained by Åqvist and Warshel [77] is more realistic. Although the authors are hesitant to criticize [76] and point out that a scaling factor of ~0.3 gives 'excellent' agreement with experiments, the fact remains that seemingly rigorous potential-of-mean-force force treatments, when used with an improper treatment of long-range interactions, produces incorrect penetration barriers (which are the most important factors in controlling ion conductance).
    • + through the gramicidin channel. This is done by comparing the calculated and observed conductance. It is found that the barriers calculated by the approach of Roux and Karplus [76] drastically overestimate the actual barrier whereas the profile obtained by Åqvist and Warshel [77] is more realistic. Although the authors are hesitant to criticize [76] and point out that a scaling factor of ~0.3 gives 'excellent' agreement with experiments, the fact remains that seemingly rigorous potential-of-mean-force force treatments, when used with an improper treatment of long-range interactions, produces incorrect penetration barriers (which are the most important factors in controlling ion conductance).
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    • The effect of protein relaxation on charge - Charge interactions and dielectric constants in proteins
    • in press
    • Sham YY, Muegge I, Warshel A. The effect of protein relaxation on charge - charge interactions and dielectric constants in proteins. Biophys J. 1998;. in press.
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    • Incorporating protein conformational flexibility into the calculation of pH-dependent protein properties
    • Alexov EG, Gunner MR. Incorporating protein conformational flexibility into the calculation of pH-dependent protein properties. Biophys J. 72:1997;2075-2093.
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    • Microscopic models for quantum mechanical calculations of chemical processes in solution
    • Luzhkov V, Warshel A. Microscopic models for quantum mechanical calculations of chemical processes in solution. J Comput Chem. 13:1992;199-213.
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    • Luzhkov, V.1    Warshel, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.