Pages that link to "Q46153921"

The following pages link to Thermodynamics of model prions and its implications for the problem of prion protein folding (Q46153921):

Displaying 42 items.

• A method to assess compositional bias in biological sequences and its application to prion-like glutamine/asparagine-rich domains in eukaryotic proteomes (Q24796241) (← links)
• A minimal sequence code for switching protein structure and function (Q27658235) (← links)
• Reversible formation of on-pathway macroscopic aggregates during the folding of maltose binding protein (Q28344778) (← links)
• Phase diagrams describing fibrillization by polyalanine peptides (Q28386736) (← links)
• Spontaneous fibril formation by polyalanines; discontinuous molecular dynamics simulations (Q28393682) (← links)
• Heparin binding confers prion stability and impairs its aggregation (Q33613234) (← links)
• A minimalist model protein with multiple folding funnels (Q33929722) (← links)
• Apoptosis modulators in the therapy of neurodegenerative diseases (Q34074800) (← links)
• alpha-helix formation: discontinuous molecular dynamics on an intermediate-resolution protein model (Q34084053) (← links)
• Folding thermodynamics of model four-strand antiparallel beta-sheet proteins (Q34177130) (← links)
• The role of dimerization in prion replication (Q34177517) (← links)
• Assembly and kinetic folding pathways of a tetrameric beta-sheet complex: molecular dynamics simulations on simplified off-lattice protein models (Q34184303) (← links)
• Self-assembly of the ionic peptide EAK16: the effect of charge distributions on self-assembly (Q34186646) (← links)
• A structural model of polyglutamine determined from a host-guest method combining experiments and landscape theory (Q34187126) (← links)
• Helical ambivalency induced by point mutations (Q34723714) (← links)
• The role of side-chain interactions in the early steps of aggregation: Molecular dynamics simulations of an amyloid-forming peptide from the yeast prion Sup35 (Q34982192) (← links)
• Modeling evolutionary landscapes: mutational stability, topology, and superfunnels in sequence space (Q35629685) (← links)
• Contact-induced structure transformation in transmembrane prion propagation (Q35696483) (← links)
• Effects of macromolecular crowding on biochemical reaction equilibria: a molecular thermodynamic perspective. (Q35940113) (← links)
• Solvent-amino acid interaction energies in three-dimensional-lattice Monte Carlo simulations of a model 27-mer protein: Folding thermodynamics and kinetics (Q36526437) (← links)
• Exploring protein aggregation and self-propagation using lattice models: phase diagram and kinetics (Q36639277) (← links)
• Conformational propagation with prion-like characteristics in a simple model of protein folding (Q36640333) (← links)
• Design of therapeutic proteins with enhanced stability. (Q37274488) (← links)
• Redesigning the hydrophobic core of a model beta-sheet protein: destabilizing traps through a threading approach (Q40780634) (← links)
• Generation of prions in vitro and the protein-only hypothesis (Q41862923) (← links)
• Solvent effects on the conformational transition of a model polyalanine peptide (Q42037889) (← links)
• The natural silk spinning process. A nucleation-dependent aggregation mechanism? (Q42052702) (← links)
• Accounting for Protein-Solvent Contacts Facilitates Design of Nonaggregating Lattice Proteins (Q42267442) (← links)
• Optimal region of average side-chain entropy for fast protein folding (Q42847498) (← links)
• Protein aggregation determinants from a simplified model: cooperative folders resist aggregation (Q43093815) (← links)
• Thermodynamics and stability of a beta-sheet complex: molecular dynamics simulations on simplified off-lattice protein models (Q43104919) (← links)
• Thermodynamics of folding and association of lattice-model proteins (Q44180316) (← links)
• Effect of rate of chemical or thermal renaturation on refolding and aggregation of a simple lattice protein (Q44856188) (← links)
• Exploring the essential collective dynamics of interacting proteins: application to prion protein dimers (Q45760615) (← links)
• Sequence-dependent dynamical instability of the human prion protein: a comparative simulation study (Q47861173) (← links)
• Coupled folding-binding versus docking: a lattice model study (Q51642594) (← links)
• Effects of macromolecular crowding on protein folding and aggregation studied by density functional theory: statics (Q52031195) (← links)
• The role of hydrophobicity patterns in prion folding as revealed by recurrence quantification analysis of primary structure (Q52081278) (← links)
• To What Extent Are the Terminal Stages of Sepsis, Septic Shock, Systemic Inflammatory Response Syndrome, and Multiple Organ Dysfunction Syndrome Actually Driven by a Prion/Amyloid Form of Fibrin? (Q53723228) (← links)
• Head-to-tail and side-by-side oligomerization of human carbonic anhydrase II: a small angle X-ray scattering study (Q73408875) (← links)
• Effects of macromolecular crowding on protein folding and aggregation studied by density functional theory: dynamics (Q78751373) (← links)
• A lattice protein with an amyloidogenic latent state: stability and folding kinetics (Q79814158) (← links)