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Effects of Crowding and Confinement on the Structures of the Transition State Ensemble in Proteins
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
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Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical features
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THE weighted histogram analysis method for free‐energy calculations on biomolecules. I. The method
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Multiple protein folding nuclei and the transition state ensemble in two‐state proteins
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Structure of Met‐enkephalin in explicit aqueous solution using replica exchange molecular dynamics
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Lattice models for proteins reveal multiple folding nuclei for nucleation-collapse mechanism 1 1Edited by A. R. Fersht
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Exploring the kinetic requirements for enhancement of protein folding rates in the GroEL cavity
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Mapping the transition state of the WW domain β-sheet
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The folding mechanism of a β-sheet: the WW domain
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Effects of pH, Salt, and Macromolecular Crowding on the Stability of FK506-binding Protein: An Integrated Experimental and Theoretical Study
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Symmetric Connectivity of Secondary Structure Elements Enhances the Diversity of Folding Pathways
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Nanopore–Protein Interactions Dramatically Alter Stability and Yield of the Native State in Restricted Spaces
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Replica-exchange molecular dynamics method for protein folding
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Effect of Dextran on Protein Stability and Conformation Attributed to Macromolecular Crowding
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Structural properties of lipid-binding sites in cytoskeletal proteins
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Protein folding funnels: the nature of the transition state ensemble
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Protein folding kinetics: timescales, pathways and energy landscapes in terms of sequence-dependent properties
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Exploring the Interplay between Topology and Secondary Structural Formation in the Protein Folding Problem
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inferredcites →https://doi.org/10.1073/pnas.0731771100openalex-snapshot
The structural basis for biphasic kinetics in the folding of the WW domain from a formin-binding protein: Lessons for protein design?
inferredcites →https://doi.org/10.1073/pnas.1831920100openalex-snapshot
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FlgM gains structure in living cells
inferredcites →https://doi.org/10.1073/pnas.97.2.634openalex-snapshot
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inferredcites →https://doi.org/10.1103/physrevlett.68.2696openalex-snapshot
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Macromolecular Crowding: Biochemical, Biophysical, and Physiological Consequences
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Models for Excluded Volume Interaction between an Unfolded Protein and Rigid Macromolecular Cosolutes: Macromolecular Crowding and Protein Stability Revisited
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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Macromolecular Crowding Modulates Folding Mechanism of α/β Protein Apoflavodoxin
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Dependence of Protein Folding Stability and Dynamics on the Density and Composition of Macromolecular Crowders
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