Jove
Visualize
联系我们
JoVE
x logofacebook logolinkedin logoyoutube logo
关于 JoVE
概览领导团队博客JoVE 帮助中心
作者
出版流程编辑委员会范围与政策同行评审常见问题投稿
图书馆员
用户评价订阅访问资源图书馆顾问委员会常见问题
研究
JoVE JournalMethods CollectionsJoVE Encyclopedia of Experiments存档
教育
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab Manual教师资源中心教师网站
使用条款与条件
隐私政策
政策

相关概念视频

Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

3.1K
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
3.1K
Cytoskeletal Proteins in Bacteria01:29

Cytoskeletal Proteins in Bacteria

4.4K
Bacterial cells were initially considered simple, randomly organized structures lacking a cytoskeleton. However, the discovery of cytoskeleton homologs in bacteria led to the change of this opinion. Bacterial cytoskeletal filaments regulate the cell shape, cell polarity, cell division, and partitioning of plasmids during cell division. It was later discovered that bacterial cytoskeletal proteins, mainly actin and tubulin homologs, are diverse compared to their eukaryotic counterparts. On the...
4.4K
Structure of Porins01:21

Structure of Porins

4.1K
Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel...
4.1K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

20.8K
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
20.8K
Valence Bond Theory02:42

Valence Bond Theory

11.6K
Coordination compounds and complexes exhibit different colors, geometries, and magnetic behavior, depending on the metal atom/ion and ligands from which they are composed. In an attempt to explain the bonding and structure of coordination complexes, Linus Pauling proposed the valence bond theory, or VBT, using the concepts of hybridization and the overlapping of the atomic orbitals. According to VBT, the central metal atom or ion (Lewis acid) hybridizes to provide empty orbitals of suitable...
11.6K
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

693
Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
693

您也可能阅读

相关文章

通过共同作者、期刊和引用图与本文相关的文章。

排序
Same author

Transition Metal Activation Reframes SAMHD1 Regulation.

ACS chemical biology·2026
Same author

Topological imaging of single-cell CAF heterogeneity for predicting prognosis and adjuvant chemotherapy benefit in pancreatic cancer.

European journal of radiology·2026
Same author

Structure-bioactivity relationships in lignins: A multivariate analysis.

International journal of biological macromolecules·2026
Same author

Discovery of a [4Fe-4S] cluster in the PRRSV Nsp1α leader protease reveals host-virus interplay in its downstream functions.

Science advances·2026
Same author

Multi-lab, multi-enzyme study demonstrates the versatility of bacterial microcompartment shells as a modular platform for confined biocatalysis.

Metabolic engineering·2026
Same author

Amino Acids in the RSSY Motif of Lipoyl Synthase Control Substrate Binding and Reactivity.

bioRxiv : the preprint server for biology·2026

相关实验视频

Updated: Mar 28, 2026

Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry
14:58

Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry

Published on: November 12, 2012

48.9K

细菌微区块蛋白的结构和功能 设计用于结合 [4Fe-4S] 集群

Clément Aussignargues, Maria-Eirini Pandelia1, Markus Sutter2

  • 1Department of Chemistry, The Pennsylvania State University , University Park, Pennsylvania 16802, United States.

Journal of the American Chemical Society
|December 26, 2015
PubMed
概括

研究人员设计了一种细菌微分区 (BMC) 蛋白来导电. 这项创新使得生物技术应用的新型生物反应器的创建成为可能.

更多相关视频

Formation of Biomembrane Microarrays with a Squeegee-based Assembly Method
07:56

Formation of Biomembrane Microarrays with a Squeegee-based Assembly Method

Published on: May 8, 2014

14.2K
Directed Protein Packaging within Outer Membrane Vesicles from Escherichia coli: Design, Production and Purification
10:21

Directed Protein Packaging within Outer Membrane Vesicles from Escherichia coli: Design, Production and Purification

Published on: November 16, 2016

14.0K

相关实验视频

Last Updated: Mar 28, 2026

Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry
14:58

Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry

Published on: November 12, 2012

48.9K
Formation of Biomembrane Microarrays with a Squeegee-based Assembly Method
07:56

Formation of Biomembrane Microarrays with a Squeegee-based Assembly Method

Published on: May 8, 2014

14.2K
Directed Protein Packaging within Outer Membrane Vesicles from Escherichia coli: Design, Production and Purification
10:21

Directed Protein Packaging within Outer Membrane Vesicles from Escherichia coli: Design, Production and Purification

Published on: November 16, 2016

14.0K

科学领域:

  • 生物化学
  • 结构生物学
  • 生物技术

背景情况:

  • 细菌微分区 (BMC) 是以蛋白质为基础的有机体,具有透的外,对生物反应器有用.
  • 跨越BMC外的电子转移对于封装氧化还原反应至关重要.

研究的目的:

  • 为生物反应器应用设计一种能够进行电子转移的BMC外蛋白.
  • 在BMC外蛋白中创建一个功能 [4Fe-4S] 集群结合位点.

主要方法:

  • 确定BMC外蛋白组成部分的晶体结构.
  • 设计并包含一个 [4Fe-4S] 聚合点.
  • 解决了包含金属中心的工程蛋白质的结构.
  • 使用光学和EPR光谱对 [4Fe-4S] 星团进行了鉴定.

主要成果:

  • 设计的BMC外蛋白成功地结合了4Fe-4S集群.
  • 用金属中心的工程蛋白质的结构得到了1.8 Å的分辨率.
  • [4Fe-4S]集群具有较低的还原潜力 (-370 mV与SHE相比) 和通过氧化还原循环的稳定性.
  • 集群的稳定性归因于蛋白质支架的结网络.

结论:

  • 设计的BMC外蛋白为电子转移功能提供了基础.
  • 这项工作为开发具有可调节电子转移特性的先进生物反应器铺平了道路.
  • 这些发现提供了关于蛋白质支架内的金属中心结合的见解.