関連する実験動画
Updated: Jul 12, 2026
08:09
Mapping the Binding Site of an Aptamer on ATP Using MicroScale Thermophoresis
Published on: January 8, 2017
水中のATPの分子認識のために設計されたベータ-ヘアピンペプチド
Sara M Butterfield1, Marcey L Waters
1Department of Chemistry, University of North Carolina at Chapel Hill, CB 3290, Chapel Hill, North Carolina 27599, USA.
Journal of the American Chemical Society
|August 9, 2003
まとめ
設計されたペプチドは,アロマティックおよび静電力を用いてアデノシントリフォスファート (ATP) を結合します. このミニマリストなシステムは,タンパク質と核酸の認識における重要な相互作用を明らかにします.
科学分野:
- バイオケミストリー バイオケミストリー
- 分子生物学は分子生物学である.
- 化学生物学 化学生物学とは
背景:
- タンパク質と核酸の認識は,生物学的プロセスにとって極めて重要です.
- 分子認識を推進する基本的な相互作用を理解することは不可欠です.
- ミニマリストのペプチドシステムは,複雑な生物学的相互作用の洞察を提供します.
研究 の 目的:
- アデノシン三リン酸 (ATP) 結合のためのミニマリストなペプチドシステムを設計し,特徴づけること.
- ペプチド-ヌクレオチド認識における異なる相互作用タイプのエネルギー貢献を調査する.
- 分子認識におけるベータシート表面の潜在能力を探求する.
主な方法:
- トリプトファンカップルの12残留ベータヘアピンによるデノボペプチド設計.
- 結合親和度を決定するための同熱定位熱計 (ITC) または類似の方法.
- 陽子核磁共鳴 (NMR) スペクトロスコーピーは,結合モードを明らかにします.
- エネルギー貢献を定義するための計算分析.
主要な成果:
- 設計された12残留ベータ-ヘアピンペプチドは,ATP結合 afinity (5800 M-1) を有意に示した.
- 陽子NMRは,対角トリプトファン残基間のアデニンリングのインターキャラが確認されました.
- アロマティック相互作用が約 -1.8 kcal/mol,静電相互作用がそれぞれ ~ -1 kcal/mol を貢献した.
結論:
- 設計されたβ-ヘアピンペプチドは,水溶液中のATPのようなニュクレオチドを効果的に結合することができます.
- アロマティックと静電相互作用は,ペプチド-ニュクレオチド認識において重要な役割を果たします.
- このミニマリストなシステムは,タンパク質と核酸の相互作用のエネルギー学を研究するための貴重なプラットフォームを提供します.
さらに関連する動画
09:04Sequence-specific and Selective Recognition of Double-stranded RNAs over Single-stranded RNAs by Chemically Modified Peptide Nucleic Acids
Published on: September 21, 2017
10:26Biotinylated Cell-penetrating Peptides to Study Intracellular Protein-protein Interactions
Published on: December 20, 2017
関連する概念動画
01:08Hydrolysis of ATP
The bonds of adenosine triphosphate (ATP) can be broken through the addition of water, releasing one or two phosphate groups in an exergonic process called hydrolysis. This reaction liberates the energy in the bonds for use in the cell—for instance, to synthesize proteins from amino acids.
If one phosphate group is removed, a molecule of ADP—adenosine diphosphate—remains, along with inorganic phosphate. ADP can be further hydrolyzed to AMP—adenosine monophosphate—by the removal of a second...
If one phosphate group is removed, a molecule of ADP—adenosine diphosphate—remains, along with inorganic phosphate. ADP can be further hydrolyzed to AMP—adenosine monophosphate—by the removal of a second...
01:27ATP Driven Pumps I: An Overview
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 are...
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 are...
01:18ATP Synthase: Structure
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...
01:25Aquaporins
Aquaporins or AQPs are a family of integral membrane proteins whose primary function is to transport water, while some called aquaglyceroporins also transport glycerol. In addition, aquaporins have also been suspected to be involved in transporting volatile substances, such as carbon dioxide and ammonia, across membranes. Such AQPs that act as gas channels are often highly expressed in cells involved in the gaseous exchange, such as red blood cells, epithelial cells, and pulmonary capillaries.
01:19Allosteric Proteins-ATCase
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 pathway,...
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 pathway,...
01:09Multi-pass Transmembrane Proteins and β-barrels
In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...