関連する実験動画

Updated: Jul 2, 2026

Determining the Ice-binding Planes of Antifreeze Proteins by Fluorescence-based Ice Plane Affinity
08:46

Determining the Ice-binding Planes of Antifreeze Proteins by Fluorescence-based Ice Plane Affinity

Published on: January 15, 2014

アンチフリーズタンパク質の周りの水分化層の二重機能は,原子学的分子ダイナミクスシミュレーションによって明らかになりました

David R Nutt1, Jeremy C Smith

  • 1Computational Molecular Biophysics, IWR, Im Neuenheimer Feld 368, University of Heidelberg, 69120 Heidelberg, Germany. d.nutt@reading.ac.uk

Journal of the American Chemical Society
|September 9, 2008
PubMed
まとめ

スプライス・ブドワームのアンチフリーズタンパク質は,氷を結合するために一面にオーダーされた水を使用し,他の面に水を乱すことは,さらなる氷の成長を防ぐ. この二重の水の役割は,抗凍結タンパク質の機能の鍵です.

さらに関連する動画

A Microfluidic Approach for the Study of Ice and Clathrate Hydrate Crystallization08:01

A Microfluidic Approach for the Study of Ice and Clathrate Hydrate Crystallization

Published on: August 18, 2022

Identification of Plant Ice-binding Proteins Through Assessment of Ice-recrystallization Inhibition and Isolation Using Ice-affinity Purification09:43

Identification of Plant Ice-binding Proteins Through Assessment of Ice-recrystallization Inhibition and Isolation Using Ice-affinity Purification

Published on: May 5, 2017

関連する概念動画

Aquaporins01:25

Aquaporins

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.
Aqueous Solutions and Heats of Hydration02:42

Aqueous Solutions and Heats of Hydration

Water and other polar molecules are attracted to ions. The electrostatic attraction between an ion and a molecule with a dipole is called an ion-dipole attraction. These attractions play an important role in the dissolution of ionic compounds in water.
When ionic compounds dissolve in water, the ions in the solid separate and disperse uniformly throughout the solution because water molecules surround and solvate the ions, reducing the strong electrostatic forces between them. This process...
Protein Folding01:22

Protein Folding

Overview
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...
Intermolecular Forces03:13

Intermolecular Forces

Atoms and molecules interact through bonds (or forces): intramolecular and intermolecular. The forces are electrostatic as they arise from interactions (attractive or repulsive) between charged species (permanent, partial, or temporary charges) and exist with varying strengths between ions, polar, nonpolar, and neutral molecules. The different types of intermolecular forces are ion–dipole, dipole–dipole, hydrogen bonds, and dispersion; among these, dipole–dipole, hydrogen bonds, and dispersion...
Aldehydes and Ketones with Water: Hydrate Formation01:20

Aldehydes and Ketones with Water: Hydrate Formation

An oxygen-based nucleophile, like water, can undergo addition reactions with aldehydes and ketones. The reaction leads to the formation of hydrates, also referred to as 1,1-diols or geminal diols.
The formation of hydrates is a reversible reaction. Hydrate formation is influenced by steric and electronic factors accompanying the alkyl substituents on the carbonyl group: The rate of hydrate formation increases with a decrease in the number of alkyl groups attached to the carbonyl carbon. Hence,...