含有Oxazolidin-2-one的伪,可以折叠成贝塔曲的带螺旋
Claudia Tomasini1, Gianluigi Luppi, Magda Monari
1Dipartimento di Chimica G. Ciamician, Alma Mater Studiorum Università di Bologna, Via Selmi 2, 40126 Bologna, Italy. claudia.tomasini@unibo.it
Journal of the American Chemical Society
|February 16, 2006
概括
合成和分析了具有特定氧化丁 (Oxd) 部分的寡合体. B组的寡合体显示出形成有序β-曲带螺旋结构的能力,这是一种3(10) -螺旋子类型.
科学领域:
- 酸的化学结构
- 超分子化学 超分子化学
- 有机合成 有机合成
背景情况:
- 合成了含有4-carboxy-5-methyloxazolidin-2-one (Oxd) 部分的寡合体.
- 研究这些寡合物的折叠成有序结构对于理解它们的特性至关重要.
研究的目的:
- 合成和分析三组含有Oxd部分的寡合物.
- 为了确定这些寡合体是否可以折叠成有序结构.
- 为了确定折叠的寡合体所采用的特定的二次结构.
主要方法:
- 三个寡合体集的合成:Boc- ((L-Ala-L-Oxd) ((n) -OR,Boc- ((L-Ala-D-Oxd) ((n) -OR,以及Boc- ((Aib-L-Oxd) ((n) -OR.
- 使用红外吸收,核磁共振和循环二极化 (CD) 光谱分析偏好形状的分析.
- 评估稳定效应,包括Oxd部分刚性,分子内H键和C=O...H-N H键.
主要成果:
- 确定了三种稳定作用:刚性Oxd部分 (转变形状),Oxd C=O...H-(alpha) C H-键,以及1 $\leftarrow$ 4分子内C=O...H-N H-键.
- 只有B组寡合体[Boc-(L-Ala-D-Oxd) ((n) -OR) ]满足了所有三个稳定要求.
- CD光谱分析显示,B组寡合体采用β-曲丝带螺旋二次结构,是一种3(10) -螺旋子类型.
结论:
- B组的寡合体表现出一种倾向于有序的结构形成.
- 鉴定到的二次结构是一个β-曲的丝带螺旋,一种特定类型的3(10) -螺旋.
- 这项研究阐明了含有Oxd的寡合体的结构偏好.
相关概念视频
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...
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...
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 tetrahedral value,...
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 tetrahedral value,...
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 staggered...
The hydrogen atoms linked to carbons are arranged in two different axial and equatorial orientations to achieve this staggered...
Multi-pass Transmembrane Proteins and β-barrels
In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
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...
Fimbriae, Pili, and Axial Filaments
Fimbriae and pili are specialized bacterial surface structures that play pivotal roles in adhesion, genetic exchange, and motility. Composed primarily of pilin protein, these hairlike appendages are crucial for bacterial survival and pathogenicity in various environments.Fimbriae: Adhesion and PathogenicityFimbriae are fine, filamentous structures measuring 2–10 nanometers in diameter and are densely distributed on the bacterial cell surface. They facilitate bacterial adhesion to abiotic...
Peptidoglycan Synthesis
Structure of PeptidoglycanPeptidoglycan is a vital structural component of the bacterial cell wall, providing mechanical strength and shape to the cell. It consists of repeating units of two sugars—N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM)—linked by β-1,4 glycosidic bonds. These sugar chains are cross-linked by short peptide chains, forming a mesh-like polymer that surrounds the bacterial plasma membrane.Cytoplasmic Phase – Precursor SynthesisPeptidoglycan biosynthesis begins in...


