Search results
Results from the WOW.Com Content Network
Proteomics enables the identification of ever-increasing numbers of proteins. This varies with time and distinct requirements, or stresses, that a cell or organism undergoes. [3] Proteomics is an interdisciplinary domain that has benefited greatly from the genetic information of various genome projects, including the Human Genome Project. [4]
Bioinformatics is the name given to these mathematical and computing approaches used to glean understanding of biological processes. Common activities in bioinformatics include mapping and analyzing DNA and protein sequences, aligning DNA and protein sequences to compare them, and creating and viewing 3-D models of protein structures.
Proteomics pertains to protein expression profiling i.e. which proteins are expressed in the lysate of a particular cell. Protein functional analysis is the identification of protein–protein interactions (e.g. identification of members of a protein complex), protein–phospholipid interactions, small molecule targets, enzymatic substrates ...
Its main goal is to provide user-friendly, high-throughput data processing services to analyse proteomics liquid chromatography-mass spectrometry (LC-MS) data based on open source tools or tools developed and available within the platform members and build an infrastructure that will make possible for non-experts i.e. wet lab scientists to run ...
Machine learning in bioinformatics is the application of machine learning algorithms to bioinformatics, [1] including genomics, proteomics, microarrays, systems biology, evolution, and text mining. [ 2 ] [ 3 ]
Structural bioinformatics is the branch of bioinformatics that is related to the analysis and prediction of the three-dimensional structure of biological macromolecules such as proteins, RNA, and DNA. It deals with generalizations about macromolecular 3D structures such as comparisons of overall folds and local motifs, principles of molecular ...
The resulting research has applications in improving gene annotations, studying mutations, and understanding the effects of genetic manipulation. More recently, the joint profiling of surface proteins and mRNA transcripts from single cells by methods such as CITE-Seq and ESCAPE [ 1 ] has been referred to as single-cell proteogenomics, [ 2 ] [ 3 ...
An alpha-helix with hydrogen bonds (yellow dots) The α-helix is the most abundant type of secondary structure in proteins. The α-helix has 3.6 amino acids per turn with an H-bond formed between every fourth residue; the average length is 10 amino acids (3 turns) or 10 Å but varies from 5 to 40 (1.5 to 11 turns).