Open Journal of Biophysics

Open Journal of Biophysics

ISSN Print: 2164-5388
ISSN Online: 2164-5396
www.scirp.org/journal/ojbiphy
E-mail: ojbiphy@scirp.org
"The Rise and Fall of the Hydrophobic Effect in Protein Folding and Protein-Protein Association, and Molecular Recognition"
written by Arieh Ben-Naim,
published by Open Journal of Biophysics, Vol.1 No.1, 2011
has been cited by the following article(s):
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[6] Network Approaches to Elucidate the Determinants of Protein Topology and Stability
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[7] Intermolecular Interactions in Polyelectrolyte and Surfactant Complexes in Solution
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[8] Theoretical analysis on thermodynamic stability of chignolin
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[9] Accurate Calculation of Barnase and SNase Folding Energetics using short MD simulations and an Atomistic Model of the Unfolded Ensemble. Evaluation of Force …
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[10] Optimization Of Nuclear Magnetic Resonance Spectroscopy Methods For Measuring Protein Hydration In Reverse Micelles
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[12] The Structure of Water and Aqueous Systems
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[13] Hydrophobic‐Hydrophilic Forces in Protein Folding
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[14] A tensegrity model for hydrogen bond networks in proteins
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[15] Aqueous solution interactions with sex hormone-binding globulin and estradiol: A theoretical investigation
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[16] Effect of temperature during vital gluten adhesive preparation and application on shear-bond strength
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[17] Development of a Method for Amino Acid Sequence-based Prediction of Residues Comprising a Protein's Hydrophobic Core
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[18] Hydrogen‐Bond Cooperativity in Formamide2–Water: A Model for Water‐Mediated Interactions
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[19] Experimental Binding Energies in Supramolecular Complexes
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[20] Entropic formulation for the protein folding process: hydrophobic stability correlates with folding rates
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[21] Studying the role of cooperative hydration in stabilizing folded protein states
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[22] Solvent effects in the helix-coil transition model can explain the unusual biophysics of intrinsically disordered proteins
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[23] Protein solution thermodynamics: a quasichemical perspective of solvent effects
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[24] Free energetics of rigid body association of ubiquitin binding domains: A biochemical model for binding mediated by hydrophobic interaction
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[25] Chemical Thermodynamics: A Journey of Many Vistas
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[26] Solubilities, Fugacities and All That in Solution Chemistry
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[27] Water Mediation Is Essential to Nucleation of β‐Turn Formation in Peptide Folding Motifs
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[28] Comments on the paper “Levinthal's question revisited, and answered” by A. Ben-Naim
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[31] Water mediation is essential to nucleation of β-turn formation in peptide folding motifs
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