Energy landscapes of functional proteins are inherently risky.
about
Consensus protein designA comparison of the folding characteristics of free and ribosome-tethered polypeptide chains using limited proteolysis and mass spectrometryJosephin Domain Structural Conformations Explored by Metadynamics in Essential Coordinates.Enhanced molecular mobility of ordinarily structured regions drives polyglutamine diseaseDesigned protein reveals structural determinants of extreme kinetic stabilityProtein Frustratometer 2: a tool to localize energetic frustration in protein molecules, now with electrostaticsSmoothing a rugged protein folding landscape by sequence-based redesign.Thermodynamic and kinetic stability of the Josephin Domain closed arrangement: evidences from replica exchange molecular dynamicsRestricted access: spatial sequestration of damaged proteins during stress and aging.Force spectroscopy reveals the presence of structurally modified dimers in transthyretin amyloid annular oligomers.TMAO-Protein Preferential Interaction Profile Determines TMAO's Conditional In Vivo Compatibility.To be disordered or not to be disordered: is that still a question for proteins in the cell?Stepwise unfolding of human β2-microglobulin into a disordered amyloidogenic precursor at low pH.A thiol probe for measuring unfolded protein load and proteostasis in cells.Ligand-promoted protein folding by biased kinetic partitioning.Domain-Swapped Dimers of Intracellular Lipid-Binding Proteins: Evidence for Ordered Folding Intermediates.Outer membrane protein folding from an energy landscape perspective.Molecular chaperones maximize the native state yield on biological times by driving substrates out of equilibrium.Pathways of cellular proteostasis in aging and disease.Electrostatic lipid-protein interactions sequester the curli amyloid fold on the lipopolysaccharide membrane surface.Power of protein/tRNA functional assembly against aberrant aggregation.Adapting Secretory Proteostasis and Function Through the Unfolded Protein Response.A chemical chaperone induces inhomogeneous conformational changes in flexible proteins.Structural basis for cross-reactivity and conformation fluctuation of the major beech pollen allergen Fag s 1.Protein aggregates encode epigenetic memory of stressful encounters in individual Escherichia coli cells
P2860
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P2860
Energy landscapes of functional proteins are inherently risky.
description
2014 nî lūn-bûn
@nan
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
2014年论文
@zh
2014年论文
@zh-cn
name
Energy landscapes of functional proteins are inherently risky.
@ast
Energy landscapes of functional proteins are inherently risky.
@en
Energy landscapes of functional proteins are inherently risky.
@en-gb
type
label
Energy landscapes of functional proteins are inherently risky.
@ast
Energy landscapes of functional proteins are inherently risky.
@en
Energy landscapes of functional proteins are inherently risky.
@en-gb
prefLabel
Energy landscapes of functional proteins are inherently risky.
@ast
Energy landscapes of functional proteins are inherently risky.
@en
Energy landscapes of functional proteins are inherently risky.
@en-gb
P2860
P50
P356
P1154
2-s2.0-84924293849
P1476
Energy landscapes of functional proteins are inherently risky.
@en
P2093
Lila M Gierasch
P2860
P2888
P304
P356
10.1038/NCHEMBIO.1670
P5530
P577
2014-11-01T00:00:00Z
P6179
1045683958