通过N-H/N相互作用稳定转,循环和3-10和α螺旋中的δ/α形状的胺金字塔化
Noah J Daniecki1, Glenn P A Yap1, Neal J Zondlo1
1Department of Chemistry and Biochemistry, University of Delaware, Newark, Delaware 19716, United States.
ACS chemical biology
|October 1, 2025
概括
N-H/N 相互作用对蛋白质结构和动态至关重要. 这项研究揭示了这些相互作用本质上导致金字塔化,影响蛋白质折叠和稳定性.
科学领域:
- 蛋白质的结构和动态.
- 分子相互作用分子相互作用.
- 生物化学 生物化学
背景情况:
- 在蛋白质结构中观察到N-H/N相互作用,如转,循环和螺旋.
- 它们在蛋白质结构和动态中的确切作用尚未完全理解.
研究的目的:
- 调查N-H/N相互作用的固有性质.
- 了解它们对蛋白质结构和动态的影响.
主要方法:
- 获得一个分子的晶体结构与N-H/N相互作用.
- 在模型化合物上执行了DFT计算.
- 分析了小分子晶体结构.
- 检查了PDB的N-H/N相互作用跨规范氨基酸.
主要成果:
- 在一个晶体结构中观察到接近H···N的距离 (2.30 Å) 和显著的金字塔化 (12°).
- DFT计算证实了金字塔化和减少胺平面性是N-H/N相互作用的固有特征.
- N-H/N 相互作用降低了林 cis-trans 异构化的能量屏障.
结论:
- N-H/N 相互作用是蛋白质内在的结构元素.
- 它们影响蛋白质折叠路径和稳定性.
- 这些相互作用在所有20种规范性氨基酸中普遍存在,它们具有特定的构造.
相关概念视频
Protein Folding
126.3K
Overview
126.3K
Protein Folding
11.1K
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...
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
11.1K
Newman Projections
20.4K
Different notations are used to represent the three-dimensional structure of molecules on two-dimensional surfaces. One of the most commonly used representations is the dash-wedge formula. The dashed wedges, solid wedges, and the plane lines indicate the groups situated behind the plane, coming out of the plane, and in the plane, respectively.
The organic molecules rotate across the single bonds leading to numerous temporary three-dimensional structures of varying energy known as...
The organic molecules rotate across the single bonds leading to numerous temporary three-dimensional structures of varying energy known as...
20.4K
Protein and Protein Structure
86.9K
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...
A protein's shape is critical to its function. For example, an enzyme...
86.9K
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution
1.3K
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...
1.3K
Structure of Amines
3.2K
The hybridized nitrogen atom in amines possesses a lone pair of electrons and is bound to three substituents with a bond angle of around 108°, which is less than the tetrahedral angle of 109.5°. However, the C–N–H bond angle is slightly larger at 112°, with a carbon–nitrogen bond length of 147 pm. This carbon–nitrogen bond length of of amines is longer than the carbon–oxygen bond of alcohols (143 pm) but shorter than alkanes’ carbon–carbon bond (154 pm). These aspects are...
3.2K


