Structural Basis for Client Recognition and Activity of Hsp40 Chaperones

NIAID Data Ecosystem2026-05-02 收录

分子伴侣结构

蛋白折叠机制

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Structural Basis for Client Recognition and Activity of Hsp40 Chaperones

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2024-05-15

Figure S1 - N-Terminal Helix-Cap in α-Helix 2 Modulates β-State Misfolding in Rabbit and Hamster Prion Proteins

朊蛋白结构

蛋白折叠机制

2FO-FC electron density map at 1.5δ overlaid on the β2−α2 loops from respective structures of (A) wild-type rabbit PrP 121–230 (B) S170N mutant rabbit PrP 121–230, (C) S174N mutant rabbit PrP 121–230

Figshare2015-12-02 更新50

Crystal structure of apo GroEL

蛋白质晶体学

分子伴侣结构

Crystal structure of apo GroEL Descriptor: (4S)-2-METHYL-2,4-PENTANEDIOL, 60 kDa chaperonin, DI(HYDROXYETHYL)ETHER, ... Authors: Bartolucci, C, Lamba, D, Grazulis, S, Manakova, E, Heumann, H. Deposit

Protein Data Bank Japan2023-10-25 更新30

NMR solution structure of the Bacillus subtilis ClpC N-domain

蛋白质结构解析

分子伴侣结构

NMR solution structure of the Bacillus subtilis ClpC N-domain

NIAID Data Ecosystem10

DataSheet1_Exploring the misfolding and self-assembly mechanism of TTR (105–115) peptides by all-atom molecular dynamics simulation.pdf

淀粉样蛋白模拟

蛋白折叠机制

Pathological aggregation of essentially dissociative Transthyretin (TTR) monomers protein, driven by misfolded and self-interaction, is connected with Amyloid Transthyretin amyloidosis (ATTR) disease.

NIAID Data Ecosystem50

Microscopic interactions between water and urea and a beta-turn forming peptide

蛋白折叠机制

分子动力学模拟

The mechanisms by which proteins fold and unfold in aqueous solutions is still not well understood. Depsite urea being a common protein denaturant, there is no atomic level...

B2FIND20

Structural Basis for Client Recognition and Activity of Hsp40 Chaperones

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