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相关概念视频

Production of Pharmaceuticals01:30

Production of Pharmaceuticals

Industrial insulin production uses genetically engineered E. coli expressing a proinsulin gene controlled by a tryptophan promoter and containing a methionine linker for later cleavage. The cells also carry ampicillin resistance for selective growth. Seed cultures are stored at −80 °C and production begins by thawing a small amount to inoculate starter cultures, which are progressively scaled to a 50,000-L bioreactor. In the bioreactor, E. coli grow in nutrient-rich media under sterile, tightly...
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 sequences.
tRNA Activation02:26

tRNA Activation

Aminoacyl-tRNA synthetases are present in both eukaryotes and bacteria. Though eukaryotes have 20 different aminoacyl-tRNA synthetases to couple to 20 amino acids, many bacteria do not have genes for all of these aminoacyl-tRNA synthetases. Despite this, they still use all 20 amino acids to synthesize their proteins. For instance, some bacteria do not have the gene encoding the enzyme that couples glutamine with its partner tRNA. In these organisms, one enzyme adds glutamic acid to all of the...
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
The Proteasome02:18

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...

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相关实验视频

Updated: May 21, 2026

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
11:09

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation

Published on: August 1, 2018

由类酶激酶启用的蛋白质酸合成.

Jingjing J Ling1, Rocco L Policarpo, Amy E Rabideau

  • 1Department of Chemistry, Massachusetts Institute of Technology, 16-573a, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, USA.

Journal of the American Chemical Society
|June 13, 2012
PubMed
概括
此摘要是机器生成的。

研究人员开发了一种新的,简单的方法,使用sortase A来创建蛋白质铁,这对于蛋白质半合成至关重要. 这种技术促进了先进的蛋白质工程和结策略.

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A Novel Saturation Mutagenesis Approach: Single Step Characterization of Regulatory Protein Binding Sites in RNA Using Phosphorothioates
11:49

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Published on: August 21, 2018

相关实验视频

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Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
11:09

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation

Published on: August 1, 2018

A Novel Saturation Mutagenesis Approach: Single Step Characterization of Regulatory Protein Binding Sites in RNA Using Phosphorothioates
11:49

A Novel Saturation Mutagenesis Approach: Single Step Characterization of Regulatory Protein Binding Sites in RNA Using Phosphorothioates

Published on: August 21, 2018

科学领域:

  • 生物化学 生物化学
  • 蛋白质工程是指蛋白质的工程.
  • 合成生物学 合成生物学

背景情况:

  • 具有C端二的蛋白质是蛋白质半合成中的关键中间体.
  • 目前合成蛋白质铁的方法主要依赖于人工智能.

研究的目的:

  • 引入一种简单而常规的策略,用于制备具有C端 (α) 硫的重组蛋白质.
  • 为了证明这种方法在合成复杂蛋白质结构中的实用性.

主要方法:

  • 使用索尔塔酶A用于制备含有C端 (α) 铁的重组蛋白质.
  • 应用该方法合成了两种炭毒素载荷蛋白,一种含有 (α) 铁,另一种含有D-多片段.
  • 评估了这些变体通过保护性抗原孔的转移.

主要成果:

  • 通过使用类酶A.成功制备了与C端 (α) 铁的重组蛋白质.
  • 证明了一种含有D多片段的蛋白质在域之间合成.
  • 证实了这两种工程蛋白质变体都能通过保护性抗原孔转移.

结论:

  • 基于Sortase A的策略提供了一种简单而有效的替代方法来合成蛋白质硫.
  • 这种方法可以将类酶介导的结合与原生化学结合相结合,用于先进的蛋白质构造.
  • 开发的技术扩大了蛋白质半合成和工程复杂生物分子的可能性.