相关实验视频

Updated: Jul 27, 2025

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
11:27

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

4.0K

来自Helicobacter pylori的HtrA的晶体结构和溶液构造揭示了pH依赖的寡合转化和构造重组

Liwei Cui1, Xiangrui Shi2, Huiling Li3

  • 1Institute of Immunology, PLA, Army Medical University, Chongqing 400038, China; Department of Tropical Medicine and Infectious Diseases, Hainan Hospital of Chinese PLA General Hospital, Sanya, Hainan 572000, China.

International journal of biological macromolecules
|June 10, 2023
PubMed
概括

来自Helicobacter pylori的高温要求A (HtrA) 破坏了胃组织. 这项研究揭示了HtrA.

关键词:
符合性重新安排.在Helicobacter Pylori的研究中,在HtrA蛋白酶中,

更多相关视频

From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins09:55

From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins

Published on: July 4, 2016

13.5K
Förster Resonance Energy Transfer Mapping: A New Methodology to Elucidate Global Structural Features07:09

Förster Resonance Energy Transfer Mapping: A New Methodology to Elucidate Global Structural Features

Published on: March 16, 2022

2.6K

相关概念视频

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

At room temperature, the chair conformer of cyclohexane undergoes rapid ring flipping between two equivalent chair conformers at a rate of approximately 105 times per second. These two chair conformers are in equilibrium. The rapid ring flipping results in the interconversion of the axial proton to an equatorial proton and an equatorial to the axial proton. Such interconversions are too rapid and cannot be detected on the NMR timescale. Hence, the NMR spectrometer cannot distinguish between the...
886
Conformations of Cyclohexane02:11

Conformations of Cyclohexane

Cyclohexane does not exist in a planar form due to the high angle and torsional strain it would experience in the planar structure. Instead, it adopts non-planar chair and boat conformations.
The chair form is the most stable and derives its name from its resemblance to the “easy chair.” In the chair conformation, two carbon atoms are arranged out-of-plane — one above and one below, minimizing the torsional strain. In the chair form, the bond angle is very close to the ideal...
12.6K
Protein Folding01:22

Protein Folding

Overview
118.5K
Chair Conformation of Cyclohexane02:02

Chair Conformation of Cyclohexane

The chair conformation is the most stable form of cyclohexane due to the absence of angle and torsional strain. The absence of angle strain is a result of cyclohexane’s bond angle being very close to the ideal tetrahedral bond angle of 109.5° in its chair conformer. Similarly, the torsional strain is also absent owing to the perfectly staggered arrangement of bonds.
The hydrogen atoms linked to carbons are arranged in two different axial and equatorial orientations to achieve this...
14.8K
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...
18.1K
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...
79.8K