The 13 angstroms structure of a chaperonin GroEL-protein substrate complex by cryo-electron microscopy.
about
Cross-correlation of common lines: A novel approach for single-particle reconstruction of a structure containing a flexible domainVisualizing GroEL/ES in the Act of Encapsulating a Folding ProteinAccurate flexible fitting of high-resolution protein structures into cryo-electron microscopy maps using coarse-grained pseudo-energy minimizationAccurate flexible fitting of high-resolution protein structures to small-angle x-ray scattering data using a coarse-grained model with implicit hydration shell.Exploring the spatial and temporal organization of a cell's proteomeGroEL actively stimulates folding of the endogenous substrate protein PepQInitial evaluation of a direct detection device detector for single particle cryo-electron microscopy.Consensus among flexible fitting approaches improves the interpretation of cryo-EM data.Probing the kinetic stabilities of Friedreich's ataxia clinical variants using a solid phase GroEL chaperonin capture platform.Topologies of a substrate protein bound to the chaperonin GroELFitting multimeric protein complexes into electron microscopy maps using 3D Zernike descriptorsFollowing Natures Lead: On the Construction of Membrane-Inserted Toxins in Lipid Bilayer Nanodiscs.Go hybrid: EM, crystallography, and beyondCryo-EM and single particles.Combining efficient conformational sampling with a deformable elastic network model facilitates structure refinement at low resolution.GroEL-mediated protein folding: making the impossible, possible.Flexible fitting of high-resolution x-ray structures into cryoelectron microscopy maps using biased molecular dynamics simulationsStructural frameworks for considering microbial protein- and nucleic acid-dependent motor ATPases.A method for the alignment of heterogeneous macromolecules from electron microscopy.Bayesian analysis of individual electron microscopy images: towards structures of dynamic and heterogeneous biomolecular assemblies.Collective variable approaches for single molecule flexible fitting and enhanced sampling.ATP-driven molecular chaperone machines.Analysis of peptides and proteins in their binding to GroEL.Chaperonin complex with a newly folded protein encapsulated in the folding chamber.Inter-ring communication allows the GroEL chaperonin complex to distinguish between different substrates.Hydrophilic residues 526 KNDAAD 531 in the flexible C-terminal region of the chaperonin GroEL are critical for substrate protein folding within the central cavity.Model-based local density sharpening of cryo-EM maps.A two-domain folding intermediate of RuBisCO in complex with the GroEL chaperonin
P2860
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P2860
The 13 angstroms structure of a chaperonin GroEL-protein substrate complex by cryo-electron microscopy.
description
2005 nî lūn-bûn
@nan
2005年の論文
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2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
2005年论文
@zh
2005年论文
@zh-cn
name
The 13 angstroms structure of ...... x by cryo-electron microscopy.
@en
type
label
The 13 angstroms structure of ...... x by cryo-electron microscopy.
@en
prefLabel
The 13 angstroms structure of ...... x by cryo-electron microscopy.
@en
P2093
P1476
The 13 angstroms structure of ...... ex by cryo-electron microscopy
@en
P2093
Charles L Brooks
Edward P Gogol
Mark T Fisher
Scott Falke
P304
P356
10.1016/J.JMB.2005.02.027
P407
P577
2005-04-01T00:00:00Z