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Proteomics

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protein
thumb|A representation of the 3D structure of the protein myoglobin showing turquoise α-helices. This protein was the first to have its structure solved by [[X-ray crystallography. Toward the right-center among the coils, a prosthetic group called a heme group (shown in gray) with a bound oxygen molecule (red).]]
proteomics
300px|thumb|right|Robotic preparation of MALDI [[mass spectrometry samples on a sample carrier]]
John Michael Jumper
American chemist and AI expert
proteome
thumb|400px|General schema showing the relationships of the genome, [[transcriptome, proteome, and metabolome (lipidome).]]
fibrous protein
constitutes one of the three main types of proteins (alongside globular and membrane proteins). There are many scleroprotein superfamilies including keratin, collagen, elastin, and fibroin
Q905695
UniProt is a freely accessible database of protein sequence and functional information, many entries being derived from genome sequencing projects. It contains a large amount of information about the biological function of proteins derived from the research literature. It is maintained by the UniProt consortium, which consists of several European bioinformatics organisations and a foundation from Washington, DC, US.
protein-protein interaction
physical interactions and constructions between multiple proteins
Edman degradation
degradation
biochip
thumb|Hundreds of gel drops are visible on the biochip.
Base excision repair
DNA repair pathway
alpha-1-acid glycoprotein
thumb|363x363px|Structure of human alpha-1-acid glycoprotein (AGP1) rendered in ChimeraX using PDB ID: 3KQ0 thumb|339x339px|Structure of human alpha-1-acid glycoprotein (AGP2) rendered in ChimeraX using PDB ID: 3APU Orosomucoid (ORM) or alpha-1-acid glycoprotein (α1AGp, AGP or AAG) is an acute phase protein found in plasma. Orosomucoid was discovered over 70 years ago and belongs to the lipocalin protein family. There are two isoforms of AGP, referred to as AGP1 and AGP2. It is an alpha-globulin glycoprotein and is modulated by two polymorphic genes. It is synthesized primarily in hepatocytes
PROSITE
PROSITE is a protein database. It consists of entries describing the protein families, domains and functional sites as well as amino acid patterns and profiles in them. These are manually curated by a team of the Swiss Institute of Bioinformatics and tightly integrated into Swiss-Prot protein annotation. PROSITE was created in 1988 by Amos Bairoch, who directed the group for more than 20 years. Since July 2018, the director of PROSITE and Swiss-Prot is Alan Bridge.
protein microarray
analytical method used to track the interactions and activities of proteins
electrophoretic mobility shift assay
molecular biology technique for determining protein-nucleic acid interactions in vitro
Human Protein Atlas
database of human proteins
Human proteome project
scientific project coordinated by the Human Proteome Organization
molten globule
various types of partially folded protein states found in mildly denaturing conditions (e.g. low pH, mild denaturant, or high temperature), collapsed with some native-like secondary structure and a dynamic tertiary structure
Protein mass spectrometry
application of mass spectrometry
proteostasis
Proteostasis is the dynamic regulation of a balanced, functional proteome. The proteostasis network includes competing and integrated biological pathways within cells that control the biogenesis, folding, trafficking, and degradation of proteins present within and outside the cell. Loss of proteostasis is central to understanding the cause of diseases associated with excessive protein misfolding and degradation leading to loss-of-function phenotypes, as well as aggregation-associated degenerative disorders. Therapeutic restoration of proteostasis may treat or resolve these pathologies.
Human Proteome Folding Project
BOINC based World Community Grid volunteer computing subproject
Secretomics
Secretomics is a type of proteomics which involves the analysis of the secretome—all the secreted proteins of a cell, tissue or organism. Secreted proteins are involved in a variety of physiological processes, including cell signaling and matrix remodeling, but are also integral to invasion and metastasis of malignant cells. Secretomics has thus been especially important in the discovery of biomarkers for cancer and understanding molecular basis of pathogenesis. The analysis of the insoluble fraction of the secretome (the extracellular matrix) has been termed matrisomics.
Human Cell Atlas
project to map all cell types of humans
secretome
The secretome is the set of proteins expressed by an organism and secreted into the extracellular space. In humans, this subset of the proteome encompasses 13-20% of all proteins, including cytokines, growth factors, extracellular matrix proteins and regulators, and shed receptors. The secretome of a specific tissue can be measured by mass spectrometry and its analysis constitutes a type of proteomics known as secretomics.
Stable isotope labeling by amino acids in cell culture
Laboratory technique for quantitative proteomics