関連する実験動画

Updated: Feb 20, 2026

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
08:48

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water

Published on: April 28, 2022

2.2K

大分子タンパク質のリングの証拠は,散発した水がないところにある

Brandon T Ruotolo1, Kevin Giles, Iain Campuzano

  • 1Department of Chemistry, Lensfield Road, University of Cambridge, Cambridge CB2 1EW, UK.

Science (New York, N.Y.)
|November 19, 2005
PubMed
まとめ

タンパク質複合体は,水なしで構造を維持する. トリプトファンRNA結合タンパク質 (TRAP) のリング構造は質量スペクトロメトリでは安定しており,トリプトファンとRNAによって強化され,マクロ分子組立分析の可能性を示している.

さらに関連する動画

In Situ Characterization of Hydrated Proteins in Water by SALVI and ToF-SIMS09:48

In Situ Characterization of Hydrated Proteins in Water by SALVI and ToF-SIMS

Published on: February 15, 2016

8.9K
Small and Wide Angle X-Ray Scattering Studies of Biological Macromolecules in Solution12:53

Small and Wide Angle X-Ray Scattering Studies of Biological Macromolecules in Solution

Published on: January 8, 2013

18.8K

関連する概念動画

Protein Folding01:22

Protein Folding

Overview
128.6K
Noncovalent Attractions in Biomolecules02:35

Noncovalent Attractions in Biomolecules

Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
65.5K
The Contractile Ring02:15

The Contractile Ring

Contractile rings are composed of microfilaments and are responsible for separating the daughter cells during cytokinesis. Contractile ring assembly proceeds along with other cell cycle events; however, very few mechanistic details are known about the timing and coordination of the contractile rings with the cell cycle.
A small GTPase, RhoA, controls the function and assembly of the contractile ring. RhoA belongs to the Ras superfamily of proteins. The activation of formins by RhoA promotes...
7.4K
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
20.0K
Globular Proteins01:27

Globular Proteins

In organisms, proteins are the most abundant macromolecules. They act as the building blocks of life and play various crucial roles in the body. Proteins can be broadly classified into two distinct subtypes based on their shape and solubilities: globular proteins and fibrous proteins.
Globular proteins serve many important physiological functions, such as acting as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be soluble in the aqueous...
11.1K
Globular and Fibrous Proteins02:21

Globular and Fibrous Proteins

Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
47.4K