China
Africa
Explore chapters and articles related to this topic
Protein Adhesives
Published in A. Pizzi, K. L. Mittal, Handbook of Adhesive Technology, 2017
Charles R. Frihart, Linda F. Lorenz
The primary sequence of amino acids determines the secondary structure, which, in turn, influences the tertiary structure of a protein and the protein’s physicochemical properties. Certain sequences of amino acids can lead to either α-helix or β-sheet structures, which are called the secondary structures [22]. These secondary structures form as the protein is being synthesized, and are important for developing the native structure of the protein because they control the folding of the protein. These structures are intrachain elements and can be disrupted by heat and various chemical additives. They should not be confused with the interchain helix formed by collagen proteins and the interchain sheet crystallites that form in synthetic polymers [25].
Product Quality and Process
Published in Wei-Shou Hu, Cell Culture Bioprocess Engineering, 2020
Some protein variants bear alterations of their amino acid sequence. These alterations in the primary sequence may occur biologically through rare errors in protein or transcript processing or through chemical modification (Panel 4.8).1 Some events, mostly occurring non-biologically, alter the higher-order protein structure, such as disulfide bond scrambling or the formation of aggregates.
Prediction of RNA secondary structure based on stem region replacement using the RSRNA algorithm
Published in Computer Methods in Biomechanics and Biomedical Engineering, 2021
Chengzhen Xu, Longjian Gao, Jin Li, Longfeng Shen, Hong Liang, Kuan Luan, Xiaomin Wu
Furthermore, high-throughput sequencing technologies are widely used to examine large amounts of primary RNA sequence data, which occupy various databases (Mane et al. 2011; Lapointe and Wickens 2018; Pucker et al. 2019) and it has been shown that the tertiary structure of RNA determines its biological function, while the secondary structure is the link between the primary and tertiary structures (Van Den Born et al. 2004; Michalak et al. 2019). Thus, predicting RNA secondary structure can be used to determine its tertiary structure, which reduces experimental costs, shortens analysis time, and improves the experimental efficiency. However, because of the limitations found in traditional methods and the lack of secondary structure data, new methods are required to deeply study and predicting RNA structures using primary sequence data, which can be achieved in silico.
Surface engineering of personal protective equipments (PPEs) to prevent the contagious infections of SARS-CoV-2
Published in Surface Engineering, 2020
The SARS-CoV-2 spike glycoprotein is reported as a trimeric protein with three domains (S1, S2 and S2′) [1,8] as shown in Figure 1. S1 subunit mediates the binding/attachment with a host cell, S2 subunit assists in fusion. It consists of a total of 1273 amino acids (141.2 kDa) [3]. Based on the primary sequence (amino acids) of the spike protein, the relative contents of various types of resides are calculated. It was estimated to be 47% hydrophobic, 35% hydrophilic, 9% positively charges and 9% negatively charges residues. This indicated the hydrophobic nature of the spike glycoprotein. Isoelectric point (PI) of this protein was also calculated from its primary sequence and PI of individual amino acids [27]. PI of the protein was estimated as , here refers to the number fraction of an amino acid in the primary sequence. The PI of the SARS-CoV-2 spike glycoprotein was found to be ∼ 5.9 i.e. it acquires negative charge at the physiological pH.