The secondary structure has been define as the hydrogen bonds of the biological macromolecules in the atomic-weight structure. In proteins, the secondary structure is defined by the hydrogen bond mode between the amino groups in the main chain, that is, the hydrogen bond defined by DSSP, and does not include the hydrogen bonds between the main chain and the side chains or between the side chains. The secondary structure of nucleic acid is defined by hydrogen bonding between bases. In many RNA molecules, the secondary structure is very important for the normal function of RNA, sometimes even more important than the sequence. This can be used to analyze non-coding RNA. Using computational simulation to determine RNA's secondary structure can greatly improve the accuracy of the structure.
1. α Helix
|The α helix is the most abundant type of secondary structure in proteins.|
2. β sheet
|β sheets are formed by H bonds between an average of 5–10 consecutive amino acids in one portion of the chain with another 5–10 farther down the chain.|
|Loops are regions of a protein chain that are 1) between α helices and β sheets, 2) of various lengths and three-dimensional configurations, and 3) on the surface of the structure.|
|A region of secondary structure that is not an α helix, a β sheet, or a recognizable turn is commonly referred to as a coil.|
|Project name||Secondary structure analysis service|
|Samples requriements||Please provide the original file after your calculation, if you need molecular dynamics service, you can directly provide the initial structure of PDB ID, etc.|
|Detection cycle||3-5 days.|
|Service including||We provide you with raw data and calculation result analysis service.|
ComputaBio provides corresponding molecular dynamics analysis services. Structure and function are the central issues of modern molecular biology. The interaction between molecules is the cornerstone of this axis problem. The interactions between molecules mainly include covalent bonds, ionic bonds, hydrogen bonds, van der Waals forces, hydrophobic interactions, etc. The ComputaBio team has been working in this field for more than ten years, and can provide you with accurate analysis of related forces. If you have needs in this regard, please feel free to contact us.