Kinetic stability of QM-Hsp53. Effect of ligands and protein concentration.

NIAID Data Ecosystem2026-03-07 收录

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https://figshare.com/articles/dataset/_Kinetic_stability_of_QM_Hsp53_Effect_of_ligands_and_protein_concentration_/225271 数据链接链接失效反馈

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Kinetic stability of QM-Hsp53. Effect of ligands and protein concentration.

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2012-10-24

File S1 - The Key to the Extraordinary Thermal Stability of P. furiosus Holo-Rubredoxin: Iron Binding-Guided Packing of a Core Aromatic Cluster Responsible for High Kinetic Stability of the Native Structure

蛋白质力学稳定性

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Supporting information and figures. Figure S1, Panel a : Control solutions lacking ferrozine. Tube-1 contains a ferric chloride solution. Tube-2 contains ferric chloride and beta-mercaptoethanol. Tube

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BindingDB Entry 11864: 6-azaindole compounds

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配体-蛋白质相互作用

Small molecule binding data for protein Toll-like receptor 7, Toll-like receptor 8, and Toll-like receptor 9, Uniprot Q9NR96, Q9NR97, and Q9NYK1

DataCite Commons2024-05-30 更新50

Atomistic molecular dynamics trajectories of the glutamine-binding protein GlnBP

分子动力学模拟

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The directory “glnbp-complex” contains 5 simulation trajectories in Amber format starting from the ligand-bound crystal structure of GlnBP with PDB identifier 1WDN. To enable...

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Thermodynamic stability of de novo designed protein mini-binders as assessed by combined thermal and chemical denaturation - Data set

蛋白质力学稳定性

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Experimental data for the paper: "Global analysis of thermal and chemical denaturation using CheMelt: Thermodynamic dissection of highly thermostable de novo designed proteins" by Vili Lampinen; Osval

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The binding affinity from semi-flexible docking (kcal/mol) and the possibility (in parenthesis) of four types of catechins and their chemical groups binding to the S1 pocket of trypsin.

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a The possibility of ligand binding to the S1 pocket. b The possibility of different groups in each ligand binding to the S1 pocket. The binding affinity from semi-flexible docking (kcal/mol) and the

NIAID Data Ecosystem30

Kinetic stability of QM-Hsp53. Effect of ligands and protein concentration.

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