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Mass Spectrometry: Overview01:19

Mass Spectrometry: Overview

Mass spectrometry is an analytical technique used to determine the molecular mass and molecular formula of a compound. The basic principle of mass spectrometry is to generate ions from the analyte molecule and measure these ion abundances against their molecular mass. One common type of ionization, known as electron ionization or EI, bombards the analyte molecules in the gas phase with high-energy electron beams. The electron beams displace an electron from the molecule and leave behind a...
High-Resolution Mass Spectrometry (HRMS)01:15

High-Resolution Mass Spectrometry (HRMS)

The resolution of a mass spectrometer depends on the efficiency of separating ions with different ion masses. The mass of an atom is approximated to the sum of the masses of protons and neutrons inside, considering the masses of protons and neutrons as equal. However, the masses of the proton (1.6726 × 10−24 g) and neutron (1.6749 × 10−24 g) are not truly equal. There is a minor error in the expression of atomic masses relative to the simplest atom of hydrogen. For example, the mass of helium...
Mass Spectrum01:23

Mass Spectrum

A mass spectrum is the graphical representation of the relative abundance of the charged fragments in an analyte plotted against their mass-to-charge ratio (m/z). The plot's x-axis represents the ratio of the mass of the charged fragment to the number of charges it carries. The y axis of the plot represents the relative abundance of each charged species. The relative abundance is calculated from the signal intensity of each charged species recorded at the detector. The most intense signal (the...
Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
MALDI-TOF Mass Spectrometry01:19

MALDI-TOF Mass Spectrometry

Mass spectrometry is a powerful characterization technique that can identify and separate a wide variety of compounds ranging from chemical to biological entities, based on their mass-to-charge ratio (m/z). The instruments that allow this detection, known as mass spectrometers, have three components: an ion source, a mass analyzer, and a detector. These spectrometers differ based on the nature of their ion source and analyzers.Matrix-assisted laser desorption ionization (MALDI) is a commonly...

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Mass-Sensitive Particle Tracking to Characterize Membrane-Associated Macromolecule Dynamics
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Mass-Sensitive Particle Tracking to Characterize Membrane-Associated Macromolecule Dynamics

Published on: February 18, 2022

単一分子レベルでの質量作用

Min Ju Shon1, Adam E Cohen

  • 1Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, USA.

Journal of the American Chemical Society
|August 15, 2012
PubMed
まとめ
この要約は機械生成です。

私たちは,小さなナノ製の穴に単分子光を用いて分子動力学を研究するための新しいシステムを開発しました. この方法は,閉じ込められた反応の統計的変動を明らかにし,大量化学を超えた新しい洞察を提供します.

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Combining Single-molecule Manipulation and Imaging for the Study of Protein-DNA Interactions

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Last Updated: May 19, 2026

Mass-Sensitive Particle Tracking to Characterize Membrane-Associated Macromolecule Dynamics
13:30

Mass-Sensitive Particle Tracking to Characterize Membrane-Associated Macromolecule Dynamics

Published on: February 18, 2022

Single-Molecule Measurement of Protein Interaction Dynamics Within Biomolecular Condensates
06:48

Single-Molecule Measurement of Protein Interaction Dynamics Within Biomolecular Condensates

Published on: January 5, 2024

Combining Single-molecule Manipulation and Imaging for the Study of Protein-DNA Interactions
14:43

Combining Single-molecule Manipulation and Imaging for the Study of Protein-DNA Interactions

Published on: August 27, 2014

科学分野:

  • 物理化学 物理化学
  • ナノテクノロジー ナノテクノロジー
  • 化学物理 化学物理

背景:

  • 単一分子レベルで分子動力学と反応を研究することは,基本的な化学プロセスを理解するために重要である.
  • 従来の大量化学の方法は,限られたシステムや低分子数のシステムでのみ観察可能な現象をしばしば隠しています.
  • 既存の技術は,個々の分子の長期的,結合のない観察に苦労する可能性があります.

研究 の 目的:

  • 少数の分子の可逆封入のための新しいシステムを開発する.
  • 分子ダイナミクスの無添加,長期,高度な並列の研究を可能にするために.
  • 閉じ込められた幾何学における二分子反応を調査し,統計力学の現象を観察する.

主な方法:

  • 分子閉じ込めのためのナノスケールの"穴"の配列の製造.
  • ダイナミックな観察のための単分子光顕微鏡の活用.
  • 穴の内の分子集団を制御するための可逆封じ込め技術.

主要な成果:

  • 小さな分子量を逆転的に捕まえるシステムを実証した.
  • 閉じた室内の反応均衡と速度の統計的変動に関連する観測現象.
  • 室内占有率の変動から生じる安定状態の変動を特定した.

結論:

  • 開発されたシステムは,分子動力学と限られた空間での反応に関する新しい研究を促進します.
  • 統計的変動は,統計力学によって予測されているが,低分子数限定システムでは観測可能で有意になる.
  • これらの発見は,微流体学や生物学的システムを含む様々な閉じ込められた環境で起こる反応に意味を持っています.