相关实验视频

Updated: Jun 10, 2025

Microfluidic Mixers for Studying Protein Folding
12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

15.1K

来自大肠杆菌 (Escherichia coli) 的核糖体蛋白 L25 中三个不同的α-螺旋体的分子动力学

Yuri Chirgadze1, Ilya Likhachev2, Nikolai Balabaev2

  • 1Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, Russia.

Biochemistry and biophysics reports
|October 15, 2024
PubMed
概括

这项研究分析了水中的核糖体蛋白L25 (大肠杆菌) 的动态,揭示了α螺旋运动如何与侧链约束和β-sheet稳定性有关,这对蛋白质功能至关重要.

关键词:
球状蛋白质是一种球状蛋白质.分子动力学分子动力学一个α-螺旋.

更多相关视频

Single Molecule Fluorescence Energy Transfer Study of Ribosome Protein Synthesis08:07

Single Molecule Fluorescence Energy Transfer Study of Ribosome Protein Synthesis

Published on: July 6, 2021

2.6K
Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding10:50

Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding

Published on: September 15, 2010

9.6K

相关概念视频

Protein Organization01:13

Protein Organization

Overview
136.8K
Protein Folding01:22

Protein Folding

Overview
117.5K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
17.8K
Protein and Protein Structure02:15

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
78.8K
Improving Translational Accuracy02:07

Improving Translational Accuracy

Base complementarity between the three base pairs of mRNA codon and the tRNA anticodon is not a failsafe mechanism. Inaccuracies can range from a single mismatch to no correct base pairing at all. The free energy difference between the correct and nearly correct base pairs can be as small as 3 kcal/ mol. With complementarity being the only proofreading step, the estimated error frequency would be one wrong amino acid in every 100 amino acids incorporated. However, error frequencies observed in...
9.3K
Termination of Translation01:44

Termination of Translation

The large ribosomal subunit has several important structures essential to translation. These include the peptidyl transferase center (PTC) - which is the site where the peptide bond is formed - and a large, internal, water-filled tube through which the nascent polypeptide moves. This latter structure is called the Peptide Exit Tunnel, and it begins at the PTC and spans the body of the large ribosomal subunit. During translation, as the nascent polypeptide chain is synthesized, it passes through...
25.2K