相关实验视频

Updated: Jan 17, 2026

Analysis of Group IV Viral SSHHPS Using In Vitro and In Silico Methods
10:40

Analysis of Group IV Viral SSHHPS Using In Vitro and In Silico Methods

Published on: December 21, 2019

26.4K

瑞皮塞法卢斯微普拉斯三酸异相酶二聚体接口是由一个关键的氨酸残留物稳定

Luiz Saramago1, Nallely Cabrera2, Beatriz Aguirre2

  • 1Laboratório Integrado de Bioquímica Hatisaburo Masuda / NUPEM, Laboratório de Bioquímica de Artrópodes Hematófagos/ IBqM, Laboratório de Tecido Conjuntivo/ HUCCF and Centro Nacional de Biologia Estrutural e Bioimagem (CENABIO), Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil.

Biochimica et biophysica acta. General subjects
|September 14, 2025
PubMed
概括

在Rhipicephalus microplus triosephosphate isomerase (RmTIM) 中研究一种非保存的氨酸,揭示了它在酶稳定性和功能中的关键作用. 这种残留物的突变显著损害了催化效率和蛋白质结构,为虫杀虫剂的开发提供了潜在的目标.

关键词:
化学敏感性 化学敏感性氨酸 86 氨酸 86 氨酸里皮塞法卢斯 (Rhipicephalus microplus) 是一个微型.局部导向的突变发生.热稳定性 热稳定性一个提克提克,一个提克提克.三酸异构酶是一种三酸异构酶.

更多相关视频

Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors10:33

Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors

Published on: October 26, 2015

11.8K
X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep105011:27

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

4.3K

相关概念视频

Protein Modifications in the RER01:26

Protein Modifications in the RER

Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
6.9K
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
14.4K
Protein-Protein Interfaces02:04

Protein-Protein Interfaces

4.4K
Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
10.1K