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相关概念视频

ATP Driven Pumps I: An Overview01:27

ATP Driven Pumps I: An Overview

8.5K
ATP-driven pumps, also known as transport ATPases, are integral membrane proteins. They have binding sites for ATP located on the membrane's cytosolic side and the ion-conducting domain in the transmembrane region. These pumps use the free energy released from ATP hydrolysis to move the solutes across cell membranes against an electrochemical gradient.
There are four main types of ATP-driven pumps - P-type, V-type, F-type, and ABC transporter. All these pumps are of varying complexities and...
8.5K
ATP Driven Pumps II: P-type Pumps01:34

ATP Driven Pumps II: P-type Pumps

5.1K
The P-type pumps are a large family of integral membrane transporter ATPases. They are divided into five major types based on substrate specificity, from I to V.
A typical P-type pump has three cytosolic domains: nucleotide-binding (N), phosphorylation (P), and activator (A) domains. These domains are connected to the membrane-spanning helices by short amino acid segments. ATP hydrolysis and covalent phosphoenzyme intermediate formation are crucial parts of the catalytic cycle. At the highly...
5.1K
Primary Active Transport01:29

Primary Active Transport

10.8K
In contrast to passive transport, active transport involves a substance being moved through membranes in a direction against its concentration or electrochemical gradient. There are two types of active transport: primary active transport and secondary active transport. Primary active transport utilizes chemical energy from ATP to drive protein pumps embedded in the cell membrane. With energy from ATP, the pumps transport ions against their electrochemical gradients—a direction they would...
10.8K
ATP Driven Pumps III: V-type Pumps01:30

ATP Driven Pumps III: V-type Pumps

3.9K
V-type pumps are ATP-driven pumps found in the vacuolar membranes of plants, yeast, endosomal and lysosomal membranes of animal cells, plasma membranes of a few specialized eukaryotic cells, and some prokaryotes. They are also known as the V1Vo-ATPase, that couple ATP hydrolysis to transport protons against a concentration gradient.
The peripheral or cytosolic V1 domain with eight subunits is involved in ATP hydrolysis. The integral or transmembrane V0 domain containing at least five subunits...
3.9K
Membrane Asymmetry Regulating Transporters01:19

Membrane Asymmetry Regulating Transporters

4.8K
Enzymes like flippase, floppase, and scramblase transfer phospholipids from one layer to another in the membrane, thereby affecting membrane asymmetry.
Flippase
Eukaryotic flippases are type-IV P-type ATPases or P4-ATPases belonging to P-type ATPase family proteins that are membrane-bound pumps involved in the ATP-mediated transport of ions and molecules across the membrane. Flippases flip specific phospholipids from the outer to the inner leaflet of a membrane. All P4-ATPases have one...
4.8K
Energy to Drive Translocation01:37

Energy to Drive Translocation

2.1K
Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...
2.1K

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相关实验视频

Updated: Sep 1, 2025

In vitro Investigation of the MexAB Efflux Pump From Pseudomonas aeruginosa
13:40

In vitro Investigation of the MexAB Efflux Pump From Pseudomonas aeruginosa

Published on: February 17, 2014

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转amidation驱动的分子

Lorna Binks1, Chong Tian1, Stephen D P Fielden1

  • 1Department of Chemistry, University of Manchester, Oxford Road, Manchester M13 9PL, United Kingdom.

Journal of the American Chemical Society
|August 18, 2022
PubMed
概括
此摘要是机器生成的。

研究人员使用阶段性信息机制开发了新型合成分子. 这些有效地封存宏循环基质,使复杂的罗塔克桑能够在没有中间脱线的情况下得到控制的顺序组装.

更多相关视频

Expression, Detergent Solubilization, and Purification of a Membrane Transporter, the MexB Multidrug Resistance Protein
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Expression, Detergent Solubilization, and Purification of a Membrane Transporter, the MexB Multidrug Resistance Protein

Published on: December 3, 2010

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Membrane Transport Processes Analyzed by a Highly Parallel Nanopore Chip System at Single Protein Resolution
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Membrane Transport Processes Analyzed by a Highly Parallel Nanopore Chip System at Single Protein Resolution

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相关实验视频

Last Updated: Sep 1, 2025

In vitro Investigation of the MexAB Efflux Pump From Pseudomonas aeruginosa
13:40

In vitro Investigation of the MexAB Efflux Pump From Pseudomonas aeruginosa

Published on: February 17, 2014

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Expression, Detergent Solubilization, and Purification of a Membrane Transporter, the MexB Multidrug Resistance Protein
10:43

Expression, Detergent Solubilization, and Purification of a Membrane Transporter, the MexB Multidrug Resistance Protein

Published on: December 3, 2010

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Membrane Transport Processes Analyzed by a Highly Parallel Nanopore Chip System at Single Protein Resolution
11:55

Membrane Transport Processes Analyzed by a Highly Parallel Nanopore Chip System at Single Protein Resolution

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科学领域:

  • 超分子化学
  • 合成有机化学
  • 纳米技术

背景情况:

  • 分子对于受控的分子操纵至关重要.
  • 之前的方法往往缺乏有效的封存或对顺序组装缺乏控制.
  • 宏循环基质需要特定的控制结合和释放机制.

研究的目的:

  • 报告一种新型的合成分子.
  • 演示动力门的阶段性信息杆机制.
  • 为了实现宏循环基质的有效封存和受控的轮合成.

主要方法:

  • 使用了末氨基和乙烯电之间的活性模板反应.
  • 用于连续循环的碳化和碳酸转化.
  • 使用单晶X射线衍射合成的罗塔克桑的结构特征.

主要成果:

  • 开发出能够从一端或两端将宏循环连接到线程上的分子.
  • 每个循环每一个终端基团增加一个额外的环.
  • 合成了具有三种不同宏循环的 [4] 和 [5] ,通过X射线衍射证实了稳定相互作用.

结论:

  • 这种新型分子有效地利用了阶段性信息机制.
  • 缺少伪毒素状态可确保有效和可控的宏循环的顺序加载.
  • 这种方法有助于精确合成复杂的,序列定义的罗塔克桑.