一种氧化还原活性氨基酸在特定地点内被纳入蛋白质中
Lital Alfonta1, Zhiwen Zhang, Sean Uryu
1Department of Chemistry and the Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
Journal of the American Chemical Society
|December 3, 2003
概括
研究人员使用大肠杆菌中的TAG码子将 redox活性氨基酸3,4-二基-l-phenylalanine (DHP) 纳入蛋白质中. 这种DHP可以在蛋白质中通过电化学氧化,从而使新的研究和对氧化还原蛋白的工程成为可能.
科学领域:
- 生物化学和分子生物学
- 生物工程是生物工程.
- 电化学 电化学 电化学
背景情况:
- 蛋白质通常含有对其功能至关重要的氧化还原活性氨基酸.
- 非规范性氨基酸的特定位点内置允许蛋白质工程.
- 3,4-二基-l-氨 (DHP) 是一种能够进行两电子氧化的氧化还原活性氨基酸.
研究的目的:
- 选择性地和高效地将氧化还原活性氨基酸DHP纳入蛋白质中.
- 为了证明在蛋白质中内置的DHP的电化学氧化性.
- 探索研究电子转移和工程新型氧化还原蛋白的潜力.
主要方法:
- 利用大肠杆菌中的TAG码子用于特定地点的DHP的结合.
- 采用电化学方法在蛋白质结构中氧化内置的DHP.
主要成果:
- 在大肠杆菌中的蛋白质中实现了DHP的选择性和高效的结合.
- 成功地证明了DHP的电化学氧化,使其在蛋白质中的子形式.
- 验证了特定位置的氧化还原活性氨基酸结合的可行性.
结论:
- 在大肠杆菌中,对DHP的特定场所的整合是可行的.
- 嵌入的DHP保留了其氧化还原活性,并且可以通过电化学控制.
- 这种方法为研究蛋白质电子转移和设计新型氧化还原功能打开了道路.
相关概念视频
Protein Organization
Overview
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.
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.
Oxidation and Reduction of Organic Molecules
Energy production within a cell involves many coordinated chemical pathways. Most of these pathways are combinations of oxidation and reduction reactions, which occur at the same time. An oxidation reaction strips an electron from an atom in a compound, and the addition of this electron to another compound is a reduction reaction. Because oxidation and reduction usually occur together, these pairs of reactions are called redox reactions.
The removal of an electron from a molecule, results in a...
The removal of an electron from a molecule, results in a...
What are Proteins?
Proteins are polymers of amino acids linked together by peptide bonds. Proteins and polypeptides are interchangeably used to refer to long chains of amino acids. However, polypeptides have a molecular weight of fewer than 10,000 daltons, while proteins have greater molecular weight. Polypeptides with less than 20 amino acids are called oligopeptides or simply peptides. Interactions among the constituent amino acid side chains of proteins help them fold into a stable 3-dimensional structure...
Protein Organization
Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.
The primary structure of a protein is its amino acid sequence.
Protein Denaturation
The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...


