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Assessing the acid-base and conformational properties of histidine residues in human prion protein (125-228) by means of pKα calculations and molecular dynamics simulations (113 visite)

Langella E, Improta R, Crescenzi O, Barone V

Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2006 Jul 1; 64(1): 167-177.

Tipo di articolo: Journal Article,

Impact factor: 3.73

Impact factor a 5 anni: 2.964


Parole chiave: Conformational Transition, Electrostatic Calculation, Histidine Titration, Molecular Dynamics, Pkα, Prion Protein, Acid Base Balance, Article, Carboxy Terminal Sequence, Human, Molecular Model, Priority Journal, Protein Conformation, Protein Domain, Protein Structure, Proton Transport, Simulation, Titrimetry, Amino Acid Sequence, Computer Simulation, Hydrogen-Ion Concentration, Kinetics, Magnetic Resonance Spectroscopy, Peptide Fragments,

Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-33744784306&partnerID=40&md5=c76d800af03abb3d316886e04176bebb

A thorough study of the acid-base behavior of the four histidines and the other titratable residues of the structured domain of human prion protein (125-228) is presented. By using multitautomer electrostatic calculations, average titration curves have been built for all titratable residues, using the whole bundles of NMR structures determined at pH 4.5 and 7.0. According to our results, (1) only histidine residues are likely to be involved in the first steps of the pH-driven conformational transition of prion protein; (2) the pKα's of His140 and His177 are ≈7.0, whereas those of His155 and His187 are < 5.5.10-ns long molecular dynamics simulations have been performed on five different models, corresponding to the most significant combinations of histidine protonation states. A critical comparison between the available NMDR structures and our computational results (1) confirms that His155 and His187 are the residues whose protonation is involved in the conformational rearrangement of huPrP in mildly acidic condition, and (2) shows how their protonation leads to the destructuration of the C-terminal part of HB and to the loss of the last turn of HA that represent the crucial microscopic steps of the rearrangement. © 2006 Wiley-Liss, Inc.
*** IBB - CNR ***

Dipartimento di Chimica, Universitá Federico II, Complesso di Monte S. Angelo, Napoli, Italy

Istituto di Biostrutture e Bioimmagini, CNR, Napoli, Italy
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Donne, D. G., Viles, J. H., Groth, D., Mehlhorn, I., James, T. L., Cohen, F. E., Prusiner, S. B., Structure of the recombinant full-length hamster prion protein PrP (29-231): The N terminus is highly flexible (1997) Proc Natl Acad Sci USA, 94, pp. 13452-13457

Knaus, K. J., Morillas, M., Swietnicki, W., Malone, M., Surewicz, W., Yee, V. C., Crystal structure of the human prion protein reveals a mechanism for oligomerization (2001) Nat Struct Biol, 8, pp. 770-774

Haire, L. F., Whyte, S. M., Vasisht, N., Gill, A. C., Verma, C., Dodson, E. J., Dodson, G. G., The crystal structure of the globular domain of sheep prion protein (2004) J Mol Biol, 336, pp. 1175-1183

Pan, K. M., Baldwin, M., Nguyen, J., Gasset, M., Serban, A., Groth, D., Huang, Z., Conversion of -helixes into -sheets features in the formation of the scrapie prion proteins (1993) Proc Natl Acad Sci USA, 90, pp. 10962-10966

Leffers, K. W., Schell, J., Jansen, K., Lucassen, R., Kaimann, T., Nagel-Steger, L., Tatzelt, J., The structural transition of the prion protein into its pathogenic conformation is induced by unmasking hydrophobic sites (2004) J Mol Biol, 344, pp. 839-853

Armen, R. S., DeMarco, M. L., Alonso, D. O., Daggett, V., Pauling and Corey's -pleated sheet structure may define the prefibrillar amyloidogenic intermediate in amyloid disease (2004) Proc Natl Acad Sci USA, 101, pp. 11622-11627

Kelly, J. W., The environmental dependency of protein folding best explains prion and amyloid diseases (1998) Proc Natl Acad Sci USA, 95, pp. 930-932

Jackson, G. S., Hill, A. F., Joseph, C., Hosszu, L., Power, A., Waltho, J. P., Clarke, A. R., Multiple folding pathways for heterologously expressed human prion protein (1999) Biochim Biophys Acta, 1431, pp. 1-13

Alonso, D. O. V., DeArmond, S. J., Cohen, F. E., Daggett, V., Mapping the early steps in the pH-induced conformational conversion of the prion protein (2001) Proc Natl Acad Sci USA, 98, pp. 2985-2989

Alonso, D. O. V., An, C., Daggett, V., Simulations of biomolecules: Characterization of the early steps in the pH-induced conformational conversion of the hamster, bovine and human forms of the prion protein (2002) Philos Trans R Soc Lond A, 360, pp. 1165-1178

Pauly, P. C., Harris, D. A., Copper stimulates endocytosis of the prion protein (1998) J Biol Chem, 273, pp. 33107-33110

Hornshaw, M. P., McDermott, J. R., Candy, J. M., Copper binding to the N-terminal tandem repeat regions of mammalian and avian prion protein (1995) Biochem Biophys Res Commun, 207, pp. 621-629

St ckel, J., Safar, J., Wallace, A. C., Cohen, F. E., Pnisiner, S. B., Prion protein selectively binds copper (II) ions (1998) Biochemistry, 37, pp. 7185-7193

Cereghetti, G. M., Schweiger, A., Glockshuber, R., Van Doorslaer, S., Stability and Cu (II) binding of prion protein variants related to inherited human prion diseases (2003) Biophys J, 84, pp. 1985-1997

Cereghetti, M. G., Schweiger, A., Glockshuber, R., Van Doorslaer, S., Electron paramagnetic resonance evidence for binding of Cu2+ to the C-terminal domain of the murine prion protein (2001) Biophys J, 81, pp. 516-525

Ullmann, G. M., Knapp, E. -W., Electrostatic models for computing protonation and redox equilibria in proteins (1999) Eur Biophys J, 28, pp. 533-551

Cornell, W. D., Cieplak, P., Bayly, C. I., Gould, I. R., Merz Jr., K. M., Furguson, D. M., Spellmeyer, D. C., Kollman, P. A., A second generation force field for the simulation of proteins, nucleic acids, and organic molecules (1995) J Am Chem Soc, 117, pp. 5179-5197

Van Gunsteren, W. F., Berendsen, H. J. C., (1987) Gromos87 Manual, , Biomos BV, Niienborgh 4, 9747 AG Groningen, The Netherlands

Van Buuren, A. R., Marrink, S. J., Berendsen, H. J. C., A molecular dynamics study of the decane/water interface (1993) J Phys Chem, 97, pp. 9206-9212

Georgescu, R. E., Alexov, E. G., Gunner, M. R., Combining conformational flexibility and continuum electrostatics for calculating pK s in proteins (2002) Biophysical J, 83, pp. 1731-1748

Van Vlijmen, H. W., Schaefer, M., Karplus, M., Improving the accuracy of protein pK calculations: Conformational averaging versus the average structure (1998) Proteins, 33, pp. 145-158

You, T. J., Bashford, D., Conformation and hydrogen ion titration of proteins: A continuum electrostatic model with conformational flexibility (1995) Biophys J, 69, pp. 1721-1733

Ullmann, G. M., Noodelmann, L., Case, D. A., Density functional calculation of pK values and redox potentials in the bovine Rieske iron-sulfur protein (2002) J Biol Inorg Chem, 7, pp. 632-639

Ironside, J. W., Prion diseases in man (1998) J Pathol, 186, pp. 227-234

Wlodek, S. T., Antosiewicz, J., McCammon, J. A., Prediction of titration properties of structures of a protein derived from molecular dynamics trajectories (1997) Protein Sci, 6, pp. 373-382

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* Mixed metal copper(II)-nickel(II) and copper(II)-zinc(II) complexes of multihistidine peptide fragments of human prion protein (113 visite)
Jószai V, Turi I, Kállay C, Pappalardo G, Di Natale G, Rizzarelli E, Sóvágó I
J Chem Res (ISSN: 1873-3344, 0162-0134, 0162-0134print), 2012 Jul; 112: 17-24.
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* Effects of molecular dynamics and solvation on the electronic structure of molecular probes (75 visite)
Caruso P, Causà M, Cimino P, Crescenzi O, D'Amore M, Improta R, Pavone M, Rega N
Theor Chem Acc (ISSN: 1432-881x), 2012 Apr; 131(4): 1211-1212.
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* Destabilization of Lipid Membranes by a Peptide Derived from Glycoprotein gp36 of Feline Immunodeficiency Virus: A Combined Molecular Dynamics/Experimental Study (66 visite)
Merlino A, Vitiello G, Grimaldi M, Sica F, Busi E, Basosi R, D’Ursi A, Fragneto G, Paduano L, D’Errico G
J Phys Chem B (ISSN: 1520-6106, 1520-5207, 1520-5207electronic), 2012 Jan 12; 116(1): 401-412.
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* Description and Characterization of a Highly Stable Enthalpic Intermediate State in Mouse Prion Protein Folding (48 visite)
Benetti F, Biarnes X, Attanasio F, Rizzarelli E, Laio A, Legname G
Prion (ISSN: 1933-6896), 2011 Apr; 5: N/D-N/D.
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* The effect of point mutations on copper(II) complexes with peptide fragments encompassing the 106-114 region of human prion protein (96 visite)
Kállay C, Turi I, Timári S, Nagy Z, Sanna D, Pappalardo G, De Bona P, Rizzarelli E, Sóvágó I
Monatshefte Fur Chemie (ISSN: 0026-9247), 2011 Apr; 142(4): 411-419.
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* Nickel(II) complexes of the multihistidine peptide fragments of human prion protein (78 visite)
Turi I, Kállay C, Szikszai D, Pappalardo G, Di Natale G, De Bona P, Rizzarelli E, Sóvágó I
J Chem Res (ISSN: 1873-3344, 0162-0134, 0162-0134print), 2010 Sep; 104(8): 885-891.
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* Insights into Prion Protein Stability (74 visite)
Benetti F, Pastorino L, Attanasio F, Rizzarelli E, Legname G
Prion (ISSN: 1933-6896), 2010 Jul; 4(3): N/D-N/D.
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* Free-Energy Profile for CO Binding to Separated Chains of Human and Trematomus newnesi Hemoglobin: Insights from Molecular Dynamics Simulations and Perturbed Matrix Method (59 visite)
Merlino A, Vergara A, Sica F, Aschi M, Amadei A, Di Nola A, Mazzarella L
J Phys Chem B (ISSN: 1520-6106, 1520-5207, 1520-5207electronic), 2010 May 27; 114(20): 7002-7008.
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* Different Interactions Of Human And Avian Prion Proteins N-Terminal Tandem Repeat Peptides And Their Copper (ii) Complexes With Model Membranes (62 visite)
Di Natale G, Pappalardo G, Milardi D, Sciacca MFM, Attanasio F, La Mendola D, Rizzarelli E
Journal Of Chemical Physics, 2010; 114: 13830-13838.
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* Conformational preferences of the full chicken prion protein in solution and its differences with respect to mammals (73 visite)
Pietropaolo A, Muccioli L, Zannoni C, Rizzarelli E
Chemphyschem (ISSN: 1439-7641, 1439-4235, 1439-7641electronic), 2009 Jul 13; 10(9-10): 1500-1510.
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* Prion Proteins Leading to Neurodegeneration (vol 5, pg 579, 2008) (53 visite)
La Mendola D, Pietropaolo A, Pappalardo G, Zannoni C, Rizzarelli E
Current Alzheimer Research (ISSN: 1567-2050), 2009 Jun; 6(3): N/D-N/D.
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* Copper(II) complexes of prion protein PEG11-tetraoctarepeat fragment: spectroscopic and voltammetric studies (49 visite)
Bonomo RP, Di Natale G, Rizzarelli E, Tabbì G, Vagliasindi LI
Dalton Trans (ISSN: 1477-9226, 1477-7922, 1477-9234), 2009 Apr 14; (14): 2637-2646.
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* The hemoglobins of the sub-Antarctic fish Cottoperca gobio, a phyletically basal species - oxygen-binding equilibria, kinetics and molecular dynamics (83 visite)
Giordano D, Boechi L, Vergara A, Marti MA, Samuni U, Dantsker D, Grassi L, Estrin DA, Friedman JM, Mazzarella L, Di Prisco G, Verde C
Febs Journal (ISSN: 1742-464x), 2009 Apr; 276(8): 2266-2277.
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* Molecular dynamics studies of the P pilus rod subunit PapA (69 visite)
Vitagliano L, Ruggiero A, Pedone C, Berisio R
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2009 Mar; 15(3): 192-199.
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* A thermodynamic approach to the conformational preferences of the 180-195 segment derived from the human prion protein α2-helix (70 visite)
Ronga L, Palladino P, Ragone R, Benedetti E, Rossi F
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2009; 15(1): 30-35.
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* Stability of single sheet GNNQQNY aggregates analyzed by replica exchange molecular dynamics: antiparallel versus parallel association (93 visite)
Vitagliano L, Esposito L, Pedone C, De Simone A
Biochem Biophys Res Commun (ISSN: 1090-2104, 0006-291x, 1090-2104electronic), 2008 Dec 26; 377(4): 1036-1041.
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* Prion proteins leading to neurodegeneration (95 visite)
La Mendola D, Pietropaolo A, Pappalardo G, Zannoni C, Rizzarelli E
Current Alzheimer Research (ISSN: 1567-2050), 2008 Dec; 5(6): 579-590.
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* The role of the Cys2-Cys7 disulfide bridge in the early steps of Islet amyloid polypeptide aggregation: A molecular dynamics study (72 visite)
Milardi D, Pappalardo M, Pannuzzo M, Grasso DM, Rosa CL
Chemical Physics Letters (ISSN: 0009-2614), 2008 Oct 1; 463(4-6): 396-399.
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* Insights into stability and toxicity of amyloid-like oligomers by replica exchange molecular dynamics analyses (75 visite)
De Simone A, Esposito L, Pedone C, Vitagliano L
Biophysical Journal (ISSN: 1542-0086, 0006-3495), 2008 Sep 15; 95(4): 1965-1973.
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* Studies of nitric oxide interaction with mono- and dinuclear copper(II) complexes of prion protein bis-octarepeat fragments (104 visite)
Bonomo RP, Pappalardo G, Rizzarelli E, Tabbì G, Vagliasindi LI
Dalton Trans (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2008 Sep 7; (29): 3805-3816.
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* Insights into structure, stability, and toxicity of monomeric and aggregated polyglutamine models from molecular dynamics simulations (69 visite)
Esposito L, Paladino A, Pedone C, Vitagliano L
Biophysical Journal (ISSN: 1542-0086, 0006-3495), 2008 May 15; 94(10): 4031-4040.
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* Structural characterization of a neurotoxic threonine-rich peptide corresponding to the human prion protein α2-helical 180-195 segment and comparison with full-length α2-helix-derived peptides (74 visite)
Ronga L, Palladino P, Saviano G, Tancredi T, Benedetti E, Ragone R, Rossi F
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2008; 14(10): 1096-1102.
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* Time-resolved fluorescence spectroscopy and molecular dynamics simulations point out the effects of pressure on the stability and dynamics of the porcine odorant-binding protein (66 visite)
Staiano M, Saviano M, Herman P, Grycznyski Z, Fini C, Varriale A, Parracino A, Kold AB, Rossi M, D'Auria S
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2008; 89(4): 284-291.
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* An NMR and molecular dynamics investigation of the avian prion hexarepeat conformational features in solution (65 visite)
Pietropaolo A, Raiola L, Muccioli L, Tiberio G, Zannoni C, Fattorusso R, Isernia C, La Mendola D, Pappalardo G, Rizzarelli E
Chemical Physics Letters (ISSN: 0009-2614), 2007 Jul 6; 442(1-3): 110-118.
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* Nitrogen oxide interaction with copper complexes formed by small peptides belonging to the prion protein octa-repeat region (80 visite)
Bonomo RP, Pappalardo G, Rizzarelli E, Santoro AM, Tabbì G, Vagliasindi LI
Dalton Trans (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2007 Apr 14; (14): 1400-1408.
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* A Molecular Dynamics Study of Pilus Subunits: Insights into Pilus Biogenesis (87 visite)
Vitagliano L, Ruggiero A, Pedone C, Berisio R
J Mol Biol Journal Of Molecular Biology (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2007 Apr 6; 367(4): 935-941.
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* Does Tetracycline Bind Helix 2 Of Prion? An Integrated Spectroscopical And Computational Study Of The Interaction Between The Antibiotic And Alpha Helix 2 Human Prion Protein Fragments (113 visite)
Ronga L, Langella E, Palladino P, Marasco D, Tizzano B, Saviano M, Pedone C, Improta R, Ruvo M
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2007 Feb 15; 66(3): 707-715.
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* Fate of prions in soil: Interaction of a recombinant ovine prion protein with synthetic humic-like mineral complexes (59 visite)
Rao M, Russo F, Granata V, Berisio R, Zagari A, Gianfreda L
Soil Biol Biochem (ISSN: 0038-0717), 2007 Feb; 39(2): 493-504.
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* Steered molecular dynamics studies reveal different unfolding pathways of prions from mammalian and non-mammalian species (72 visite)
Pappalardo M, Milardi D, Grasso D, La Rosa C
New Journal Of Chemistry (ISSN: 1144-0546), 2007; 31(6): 901-905.
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* Molecular dynamics analyses of cross-beta-spine steric zipper models: beta-sheet twisting and aggregation (97 visite)
Esposito L, Pedone C, Vitagliano L
Proc Natl Acad Sci U S A (ISSN: 0027-8424, 1091-6490, 0027-8424print), 2006 Sep 1; 103(31): 11533-11538.
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* The prion protein: structural features and related toxic peptides (62 visite)
Ronga L, Tizzano B, Palladino P, Ragone R, Urso E, Maffia M, Ruvo M, Benedetti E, Rossi F
Chem Biol Drug Des Chemical Biology And Drug Design (ISSN: 1747-0277, 1747-0285), 2006 Sep; 68(3): 139-147.
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* The effect of the osmolyte trimethylamine N-oxide on the stability of the prion protein at low pH (46 visite)
Granata V, Palladino P, Tizzano B, Negro A, Berisio R, Zagari A
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2006 Jun 15; 82(3): 234-240.
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* Polyglutamine Repeats And Beta-Helix Structure: Molecular Dynamics Study (86 visite)
Merlino A, Esposito L, Vitagliano L
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2006 Jun 1; 63(4): 918-927.
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* Conformation analysis of aspartame-based sweeteners by NMR spectroscopy, molecular dynamics simulations, and X-ray diffraction studies (138 visite)
De Capua A, Goodman M, Amino Y, Saviano M, Benedetti E
Chembiochem (ISSN: 1439-4227, 1439-7633, 1439-7633electronic), 2006 Feb; 7(2): 377-387.
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* Prion protein misfolding: Conformational stability of the alpha 2-helix (51 visite)
Palladino P, Ronga L, Tizzano B, Rossi F, Ragone R, Tancredi T, Saviano G, Facchiano A, Costantini S, Ruvo M, Benedetti E
Understanding Biology Using Peptides, 2006; N/D: N/D-N/D.
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* The importance of dynamic effects on the enzyme activity: X-ray structure and molecular dynamics of onconase mutants (76 visite)
Merlino A, Mazzarella L, Carannante A, Di Fiore A, Di Donato A, Notomista E, Sica F
J Biol Chem Journal Of Biological Chemistry (ISSN: 0021-9258, 1083-351x), 2005 May 6; 280(18): 17953-17960.
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* The Human Prion Protein Alpha2 Helix: A Thermodynamic Study Of Its Conformational Preferences (77 visite)
Tizzano B, Palladino P, De Capua A, Marasco D, Rossi F, Benedetti E, Pedone C, Ragone R, Ruvo M
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2005 Apr 1; 59(1): 72-79.
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* Insight into ribonuclease A domain swapping by molecular dynamics unfolding simulations (63 visite)
Esposito L, Daggett V
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2005 Mar 8; 44(9): 3358-3368.
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* Open interface and large quaternary structure movements in 3D domain swapped proteins: Insights from molecular dynamics simulations of the C-terminal swapped dimer of ribonuclease (93 visite)
Merlino A, Ceruso MA, Vitagliano L, Mazzarella L
Biophysical Journal (ISSN: 0006-3495, 1542-0086), 2005 Mar; 88(3): 2003-2012.
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* Conformational properties of peptide fragments homologous to the 106-114 and 106-126 residues of the human prion protein: a CD and NMR spectroscopic study (68 visite)
Di Natale G, Impellizzeri G, Pappalardo G
Org Biomol Chem (ISSN: 1477-0520, 1477-0539, 1477-0539electronic), 2005 Feb 7; 3(3): 490-497.
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* A re-investigation of copper coordination in the octa-repeats region of the prion protein (85 visite)
Bonomo RP, Cucinotta V, Giuffrida A, Impellizzeri G, Magrì A, Pappalardo G, Rizzarelli E, Santoro AM, Tabbì G, Vagliasindi LI
Dalton Trans (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2005 Jan 7; (1): 150-158.
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* Checking the pH-induced conformational transition of prion protein by molecular dynamics simulations: Effect of protonation of histidine residues (79 visite)
Langella E, Improta R, Barone V
Biophysical Journal (ISSN: 0006-3495, 1542-0086), 2004 Dec; 87(6): 3623-3632.
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* A molecular dynamics study on the conformational stability of PrP 180-193 helix II prion fragment (67 visite)
Pappalardo M, Milardi D, La Rosa C, Zannoni C, Rizzarelli E, Grasso D
Chemical Physics Letters (ISSN: 0009-2614), 2004 Jun 1; 390(4-6): 511-516.
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* Copper(II) complexes of peptide fragments of the prion protein. Conformation changes induced by copper(II) and the binding motif in C-terminal protein region (89 visite)
Brown DR, Guantieri V, Grasso G, Impellizzeri G, Pappalardo G, Rizzarelli E
J Chem Res (ISSN: 0162-0134, 1873-3344, 0162-0134print), 2004 Jan; 98(1): 133-143.
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* Conformational conversion of prion proteins: Role synthetic PRP 173-195 fibrillogenic peptide (59 visite)
Tizzano B, Marasco D, Benedetti E, De Capua A, Palladino P, Pedone C, Perretta G, Rossi F, Ragone R, Ruvo M
Peptide Revolution, 2004; N/D: N/D-N/D.
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* Copper(II) binding of prion protein's octarepeat model peptides (86 visite)
Pappalardo G, Impellizzeri G, Campagna T
Inorg Chim Acta (ISSN: 0020-1693), 2004; 357(1): 185-194.
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* A thermodynamic and spectroscopic study on the copper(II) complexes with hexarepeats fragments of the avian prion protein (82 visite)
La Mendola D, Bonomo R, Maccarrone G, Pappalardo G, Rizzarelli E
J Chem Res (ISSN: 0162-0134, 1873-3344, 0162-0134print), 2003 Jul 15; 96(1): N/D-N/D.
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* Free energy perturbation and molecular dynamics calculations of copper binding to azurin (71 visite)
Pappalardo M, Milardi D, Grasso DM, La Rosa C
J Comput Chem (ISSN: 0192-8651, 1096-987xelectronic), 2003 Apr 30; 24(6): 779-785.
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Metal binding to prion protein (78 visite)
Bonomo RP, Grasso D, Grasso G, Guantieri V, Impellizzeri G, La Rosa C, Milardi D, Pappalardo G, Tabbì G, Rizzarelli E
Metal-Ligand Interactions - Molecular Nano- Micro- And Macro-Systems In Complex Environments, 2003 Jan 01; 116: 21-39.
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* Seeking for binding determinants of the prion protein to human plasminogen (47 visite)
Menziani MC, De Benedetti PG, Langella E, Barone V
Mol Phys (ISSN: 0026-8976), 2003; 101(17): 2763-2773.
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* Global and local motions in ribonuclease A: A molecular dynamics study (69 visite)
Merlino A, Vitagliano L, Ceruso M, Di Nola A, Mazzarella L
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2002 Nov 15; 65(4): 274-283.
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Molecular dynamics simulation in vacuo and in solution of [Aib5, 6-D- Ala8] Cyclolinopeptide A: A conformational and comparative study (56 visite)
Saviano M, Rossi F, Pavone V, Di Blasio B, Pedone C
J Biomol Struct Dyn (ISSN: 0739-1102, 1538-0254electronic, 0739-1102linking), 1992 Jun; 9(6): 1045-1060.
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67 Records (61 escludendo Abstract e Conferenze).
Impact factor totale: 225.049 (205.144 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 230.579 (209.295 escludendo Abstract e Conferenze).

Interrogazione bibliografica effettuata: (([btitle] "Conformational Transition" OR [btitle] "Electrostatic Calculation" OR [btitle] "Histidine Titration" OR [btitle] "Molecular Dynamics" OR [btitle] "Prion Protein") AND NOT [id] = 9388)







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