振动合,同位素编辑和β片结构在膜结合的多中
Cynthia Paul1, Jianping Wang, William C Wimley
1Department of Pharmacology, the Johnson Foundation for Molecular Biophysics, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
Journal of the American Chemical Society
|May 6, 2004
概括
这项研究证实了使用同位素标记和红外光谱学在脂质膜中的N-乙化六 AcWL5的反平行β片结构. 这些发现阐明了对膜结合的光谱特征负责的振动合.
科学领域:
- 生物物理学的生物物理.
- 频谱学是一种光谱学.
- 材料科学 材料科学 材料科学
背景情况:
- 众所周知,N-乙化六类WLLLLL (AcWL5) 能够分裂成脂质膜.
- 假设AcWL5在这些膜内自组装成一个反平行β-sheet结构.
研究的目的:
- 通过实验验证 membrane-bound AcWL5.5 的拟议的反平行β片结构.
- 用同位素标记来研究体结构内的振动合.
主要方法:
- (13)C同位素标记在残留2-6处的键.
- 标记的吸附在支持的脂质膜上.
- 内部反射红外光谱 (IR) 检测振动合.
- 对于平行和反平行β-sheet配置的exciton模型模拟.
主要成果:
- 在红外光谱中观察到 (13) C标记的胺I'吸收带的选择性增强.
- 实验结果与振动合的模拟结果一致.
- (13) 模型准确地复制了C频段的强度和频率.
结论:
- 膜结合的AcWL5采用一种反平行β-sheet形状.
- 观察到的光谱增强归因于跨链和内链振动合到12C模式.
- 在红外光谱学中的同位素编辑提供了对膜相关的结构洞察.
相关概念视频
Protein Organization
Overview
Mechanisms of Membrane-bending
The living membranes are flexible due to their fluid mosaic nature; however, their bending into different shapes is an active process regulated by specific lipids and proteins. The membrane bending can be transient as seen in vesicles or stable for a long time as in microvilli. Cells regulate the size, location, and duration of the membrane curvature.
Membrane bending can happen due to intrinsic changes in lipid composition or extrinsic association with different proteins. The proteins involved...
Membrane bending can happen due to intrinsic changes in lipid composition or extrinsic association with different proteins. The proteins involved...
Protein Organization
Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.
The primary structure of a protein is its amino acid sequence.
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...
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Multi-pass Transmembrane Proteins and β-barrels
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α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...
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In bromoethane, the three methyl protons are coupled to the two methylene protons that are three bonds away. In accordance with the n+1 rule, the signal from the methyl protons is split into three peaks with 1:2:1 relative intensities. The methylene protons appear as a quartet, with the relative intensities of 1:3:3:1.
Qualitatively, any spin plus-half nucleus polarizes the spins of its electrons to the minus-half state. Consequently, the paired electron in the hydrogen–carbon bond must have a...
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