代写论文:氨基酸的形成

代写论文:氨基酸的形成

一级结构是蛋白质中氨基酸的线性序列。蛋白质由20个氨基酸组成。每个氨基酸都有一个独特的侧链。氨基酸的化学是理解蛋白质结构的必要条件(Dolphin,2012)。疏水性侧链,范德华相互作用,共价键和侧链相互作用导致蛋白质结构变化。通过多种技术研究氨基酸的位置。这些解释如下(Dolphin,2012)。二级结构是α-螺旋和β-折叠。它们基于肽键的C = O和肽键的N-H基团形成。蛋白质的三维形状被认为是三级结构。蛋白质会弯曲以达到最大稳定性或最低能量状态(Leshem,2013)。中性和非极性氨基酸的疏水性侧链将蛋白质从水性介质中屏蔽掉(Dolphin,2012)。

代写论文:氨基酸的形成
发现丙氨酸,亮氨酸,缬氨酸异亮氨酸形成疏水相互作用,并发现蛋白质的芳族基团堆叠在一起。酸性和碱性氨基酸将在表面上,因为它们是亲水性的。氢键形成在影响结构的侧链中,并且发现二硫键形成序列。不同带电氨基酸之间的离子相互作用有助于结构。这是蛋白质三维结构改变的原因。在同二聚体或异二聚体中,亚基被发现是相同的。这是在第四个结构中看到的。因此,最终的形状是基于一些交互。这些都是使用多种技术进行研究的。这在下面解释。

代写论文:氨基酸的形成

Primary structure is the linear sequences of the amino acids in a protein. The proteins develop form the set of 20 amino acids. Each amino acid has a unique side chain. The chemistry of an Amino acid is imperative to understand the protein structure (Dolphin, 2012). Hydrophobic side chains, van der Waals interactions, covalent bond and side chain interactions cause the protein structure to vary. The location of the amino acids is studied by a number of techniques. These are explained in the following (Dolphin, 2012). Secondary structure is α-helix and the ß-sheet. They are formed based on the C=O of the peptide bond and the N-H group of the peptide bond. The three-dimensional shape of the protein is considered to the tertiary structure. The protein will bend to achieve maximum stability or lowest energy state (Leshem, 2013). Hydrophobic side-chains of neutral and non-polar amino acid shield the protein from the aqueous medium (Dolphin, 2012).

代写论文:氨基酸的形成
Alanine, leucine, valine isoleucine are found to form hydrophobic interactions and the aromatic groups of protein are found to stack together. Acidic and the basic amino acid will be on the surface as they are hydrophilic. Hydrogen bonds are formed in the side chain affecting the structure and the disulphide bridges are found to form sequences. Ionic interactions between the different charged amino acid contribute towards the structure. This is the reason for the 3D structure of protein to change. In the homodimer or hetero dimer, the subunits are found to be the same. This is seen in the quaternary structure. Thus, the final shape is based on a number of interactions. These are studied using a number of techniques. It is explained in the following.