Mapping the interactions present in the transition state for unfolding/folding of FKBP12.
about
Unfolding simulations reveal the mechanism of extreme unfolding cooperativity in the kinetically stable alpha-lytic proteaseN-terminal extension changes the folding mechanism of the FK506-binding proteinSimilarity and difference in the unfolding of thermophilic and mesophilic cold shock proteins studied by molecular dynamics simulationsImportant amino acid properties for determining the transition state structures of two-state protein mutants.A comparison of experimental and computational methods for mapping the interactions present in the transition state for folding of FKBP12Mechanism of protein folding.Temperature-induced unfolding of epidermal growth factor (EGF): insight from molecular dynamics simulationCapillarity-like growth of protein folding nuclei.Folding-unfolding of goat alpha-lactalbumin studied by stopped-flow circular dichroism and molecular dynamics simulations.Golden triangle for folding rates of globular proteins.A comprehensive multidimensional-embedded, one-dimensional reaction coordinate for protein unfolding/folding.Constructing, verifying, and dissecting the folding transition state of chymotrypsin inhibitor 2 with all-atom simulationsMicroscopic reversibility of protein folding in molecular dynamics simulations of the engrailed homeodomainLigand-switchable substrates for a ubiquitin-proteasome systemEarly steps in thermal unfolding of superoxide dismutase 1 are similar to the conformational changes associated with the ALS-associated A4V mutation.Dynameomics: a consensus view of the protein unfolding/folding transition state ensemble across a diverse set of protein folds.Relationship of Leffler (Bronsted) alpha values and protein folding Phi values to position of transition-state structures on reaction coordinates.Three-body interactions improve the prediction of rate and mechanism in protein folding models.Overview of protein folding mechanisms: experimental and theoretical approaches to probing energy landscapes.Restrictions to protein folding determined by the protein size.A directed approach for engineering conditional protein stability using biologically silent small molecules.The loop hypothesis: contribution of early formed specific non-local interactions to the determination of protein folding pathways.Folding intermediate and folding nucleus for I-->N and U-->I-->N transitions in apomyoglobin: contributions by conserved and nonconserved residues.Characterization of protein folding by a Φ-value calculation with a statistical-mechanical model.Structure-Based Prediction of Protein-Folding Transition Paths.Identifying critical residues in protein folding: Insights from phi-value and P(fold) analysis.Small Molecule-Induced Domain Swapping as a Mechanism for Controlling Protein Function and Assembly.What have we learned from the studies of two-state folders, and what are the unanswered questions about two-state protein folding?Transition states in protein folding kinetics: modeling phi-values of small beta-sheet proteins.How general is the nucleation-condensation mechanism?The contribution of the residues from the main hydrophobic core of ribonuclease A to its pressure-folding transition state.Co-evolutionary constraints of globular proteins correlate with their folding rates.Stability scale and atomic solvation parameters extracted from 1023 mutation experiments
P2860
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P2860
Mapping the interactions present in the transition state for unfolding/folding of FKBP12.
description
1999 nî lūn-bûn
@nan
1999 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Mapping the interactions present in the transition state for unfolding/folding of FKBP12.
@ast
Mapping the interactions present in the transition state for unfolding/folding of FKBP12.
@en
type
label
Mapping the interactions present in the transition state for unfolding/folding of FKBP12.
@ast
Mapping the interactions present in the transition state for unfolding/folding of FKBP12.
@en
prefLabel
Mapping the interactions present in the transition state for unfolding/folding of FKBP12.
@ast
Mapping the interactions present in the transition state for unfolding/folding of FKBP12.
@en
P2093
P356
P1476
Mapping the interactions present in the transition state for unfolding/folding of FKBP12.
@en
P2093
P304
P356
10.1006/JMBI.1999.2942
P407
P577
1999-08-01T00:00:00Z