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相关概念视频

Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

7.4K
Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
7.4K
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

16.0K
In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased...
16.0K
ATP Synthase: Structure01:18

ATP Synthase: Structure

16.3K
ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
16.3K
ATP Driven Pumps II: P-type Pumps01:34

ATP Driven Pumps II: P-type Pumps

5.2K
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...
5.2K
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

4.9K
Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
4.9K
Electron Transport Chain: Complex III and IV01:43

Electron Transport Chain: Complex III and IV

6.8K
During the electron transport chain, electrons from NADH and FADH2 are first transferred to complexes I and II, respectively. These two complexes then transfer the electrons to ubiquinol, which carries them further to complex III. Complex III passes the electrons across the intermembrane space to Cyt c, which carries them further to complex IV. Complex IV donates electrons to oxygen and reduces it to water. As electrons pass through complexes I, III, and IV, the energy released aids the pumping...
6.8K

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相关实验视频

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Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography
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Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography

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在同质环ATPase中的子单元间协调.

Jeffrey R Moffitt1, Yann R Chemla, K Aathavan

  • 1Department of Physics and Jason L. Choy Laboratory of Single Molecule Biophysics, University of California, Berkeley, California 94720, USA.

Nature
|January 9, 2009
PubMed
概括

研究人员直接观察了细菌phi29的DNA包装电机,这是一个环形ATPase. 他们发现它以协调的2.5个基对步骤包装DNA,每周期共计10个基对,揭示了一个新的协调机制.

科学领域:

  • 生物化学 生物化学
  • 分子生物学分子生物学
  • 结构生物学 结构生物学

背景情况:

  • 同质环ATPases是参与各种细胞过程的关键分子电机.
  • 了解它们的机制,特别是分部间协调和步骤大小,是阐明它们的功能的关键.

研究的目的:

  • 直接观察和量化细菌phi29 DNA 包装电机的子单元间协调和步骤大小.
  • 在单个分子水平上研究DNA转位的机制.

主要方法:

  • 使用高分辨率的光学子来施加力并测量phi29电机的精确运动.
  • 进行停留时间的统计分析,并应用高力来解决单个步骤.

主要成果:

  • 观察到DNA包装在10个基对 (bp) 的离散增量.
  • 揭示了每个10bp增量由四个协调的2.5bp步骤组成.
  • 证明在每个包装中,多个ATP分子在每个包装中结合和水解.

结论:

  • 菲29电机在其子单元之间表现出高度协调的水解周期,这是环ATPases的新机制.
  • 非整数的步骤大小需要开发新模型的动力-DNA相互作用.

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Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET
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