Pereira de Ara�jo, Ant�nio Francisco - Departamento de Biologia Celular, University of Brasilia

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Pereira de Ara�jo, Ant�nio Francisco - Departamento de Biologia Celular, University of Brasilia

Alternative hydrogen bond implementations produce opposite effects on collapse cooperativity of lattice homopolypeptide models
Folding protein models with a simple hydrophobic energy function: The
BIOPHYSICSAND COMPUTATIONALBIOLOGY
Jointly published by Akadmiai Kiad, Budapest Scientometrics and Springer, Dordrecht DOI: 10.1007/s11192-007-1817-6
Folding Pathway Dependence on Energetic Frustration and Interaction Heterogeneity for a Three-Dimensional
PROTEIN FOLDING COOPERATIVITY: BASIC INSIGHTS FROM MINIMALIST MODELS
Relevance of structural segregation and chain compaction for the thermodynamics of folding of a hydrophobic protein model
Non-native Interactions, Effective Contact Order, and Protein Folding: A Mutational Investigation With the
Folding simulations of a three-dimensional protein model with a nonspecific hydrophobic energy function
Folding protein models with a simple hydrophobic energy function: The fundamental importance of
Thermodynamics of Interactions between Amino Acid Side Chains: Experimental Differentiation of Aromatic-Aromatic, Aromatic-Aliphatic,
Estimates for the potential accuracy required in realistic protein folding simulations and structure recognition experiments
Monte Carlo simulations of protein folding using inexact potentials: how accurate must parameters be in order to
Description of Atomic Burials in Compact Globular Proteins by Fermi-Dirac Probability Distributions
Entropy reduction effect imposed by hydrogen bond formation on protein folding cooperativity: Evidence from a hydrophobic minimalist model
Sequence rotation in N-dimensional space and the folding of hydrophobic protein models: Surpassing the diagonal unfolded state approximation
proteinsSTRUCTURE O FUNCTION O BIOINFORMATICS Native atomic burials, supplemented by