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Structural Genomics
Structural genomics seeks to describe the Protein Structure, 3-dimensional structure of every protein encoded by a given genome. This genome-based approach allows for a high-throughput method of structure determination by a combination of protein structure prediction, experimental and modeling approaches. The principal difference between structural genomics and protein structure prediction, traditional structural prediction is that structural genomics attempts to determine the structure of every protein encoded by the genome, rather than focusing on one particular protein. With full-genome sequences available, structure prediction can be done more quickly through a combination of experimental and modeling approaches, especially because the availability of large number of sequenced genomes and previously solved protein structures allows scientists to model protein structure on the structures of previously solved homologs. Because protein structure is closely linked with protein func ...
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Protein Nuclear Magnetic Resonance Spectroscopy
Nuclear magnetic resonance spectroscopy of proteins (usually abbreviated protein NMR) is a field of structural biology in which NMR spectroscopy is used to obtain information about the structure and dynamics of proteins, and also nucleic acids, and their complexes. The field was pioneered by Richard R. Ernst and Kurt Wüthrich at the ETH, and by Ad Bax, Marius Clore, Angela Gronenborn at the NIH, and Gerhard Wagner at Harvard University, among others. Structure determination by NMR spectroscopy usually consists of several phases, each using a separate set of highly specialized techniques. The sample is prepared, measurements are made, interpretive approaches are applied, and a structure is calculated and validated. NMR involves the quantum-mechanical properties of the central core ("nucleus") of the atom. These properties depend on the local molecular environment, and their measurement provides a map of how the atoms are linked chemically, how close they are in space, and how ...
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Hi-C (genomic Analysis Technique)
] Hi-C is a high-throughput Genomics, genomic and Epigenomics, epigenomic technique to Chromosome conformation capture, capture chromatin conformation (3C). In general, Hi-C is considered as a derivative of a series of chromosome conformation capture technologies, including but not limited to 3C (chromosome conformation capture), 4C (chromosome conformation capture-on-chip/circular chromosome conformation capture), and 5C (chromosome conformation capture carbon copy). Hi-C comprehensively detects genome-wide chromatin interactions in the cell nucleus by combining 3C and massive parallel sequencing, next-generation sequencing (NGS) approaches and has been considered as a qualitative leap in C-technology (chromosome conformation capture-based technologies) development and the beginning of 3D genomics. Similar to the classic 3C technique, Hi-C measures the frequency (as an average over a cell population) at which two DNA fragments physically associate in 3D space, linking chromosomal s ...
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CATH
Cath may refer to: __NOTOC__ People * Cath Bishop (born 1971), British former rower and 2003 world champion * Cath Carroll (born 1960), British musician and music journalist * Cath Coffey (), one of the earliest members of British rap band Stereo MCs * Cath Crowley (born 1971), Australian young adult fiction author * Cath Kidston (born 1958), English fashion designer, businesswoman and author * Cath Mayo, New Zealand short story writer, novelist and musician * Cath Rae (born 1985), Scottish field hockey goalkeeper * Cath Vautier (1902–1989), New Zealand netball player, teacher and sports administrator * Cath Wallace (born 1952), New Zealand environmentalist and academic In mythology * Catha (mythology) or Cath, an Etruscan deity * Cath Palug, a feline creature in Welsh mythology Songs *" Cath...", a Death Cab for Cutie song *"Cath", a hit song by The Bluebells Other uses *Cath., abbreviation for Catholic *Catheter or catheterization * CATH, protein structure classificat ...
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Structural Classification Of Proteins
The Structural Classification of Proteins (SCOP) database is a largely manual classification of protein structural domains based on similarities of their structures and amino acid sequences. A motivation for this classification is to determine the evolutionary relationship between proteins. Proteins with the same shapes but having little sequence or functional similarity are placed in different superfamilies, and are assumed to have only a very distant common ancestor. Proteins having the same shape and some similarity of sequence and/or function are placed in "families", and are assumed to have a closer common ancestor. Similar to CATH and Pfam databases, SCOP provides a classification of individual structural domains of proteins, rather than a classification of the entire proteins which may include a significant number of different domains. The SCOP database is freely accessible on the internet. SCOP was created in 1994 in the Centre for Protein Engineering and the Lab ...
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UniProt
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, USA. The UniProt consortium The UniProt consortium comprises the European Bioinformatics Institute (EBI), the Swiss Institute of Bioinformatics (SIB), and the Protein Information Resource (PIR). EBI, located at the Wellcome Trust Genome Campus in Hinxton, UK, hosts a large resource of bioinformatics databases and services. SIB, located in Geneva, Switzerland, maintains the ExPASy (Expert Protein Analysis System) servers that are a central resource for proteomics tools and databases. PIR, hosted by the National Biomedical Research Foundation (NBRF) at the George ...
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Protein Data Bank
The Protein Data Bank (PDB) is a database for the three-dimensional structural data of large biological molecules such as proteins and nucleic acids, which is overseen by the Worldwide Protein Data Bank (wwPDB). This structural data is obtained and deposited by biologists and biochemists worldwide through the use of experimental methodologies such as X-ray crystallography, Nuclear magnetic resonance spectroscopy of proteins, NMR spectroscopy, and, increasingly, cryo-electron microscopy. All submitted data are reviewed by expert Biocuration, biocurators and, once approved, are made freely available on the Internet under the CC0 Public Domain Dedication. Global access to the data is provided by the websites of the wwPDB member organizations (PDBe, PDBj, RCSB PDB, and BMRB). The PDB is a key in areas of structural biology, such as structural genomics. Most major scientific journals and some funding agencies now require scientists to submit their structure data to the PDB. Many other ...
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Multi-drug-resistant Tuberculosis
Multidrug-resistant tuberculosis (MDR-TB) is a form of tuberculosis (TB) infection caused by bacteria that are Antimicrobial resistance, resistant to treatment with at least two of the most powerful first-line Tuberculosis management, anti-TB medications (drugs): isoniazid and rifampicin. Some forms of TB are also resistant to Tuberculosis management, second-line medications, and are called extensively drug-resistant TB (Extensively drug-resistant tuberculosis, XDR-TB). Tuberculosis is caused by infection with the bacterium ''Mycobacterium tuberculosis''. Almost one in four people in the world are infected with TB bacteria. Only when the bacteria become active do people become ill with TB. Bacteria become active as a result of anything that can reduce the person's Immunity (medical), immunity, such as HIV, advancing age, diabetes or other immunocompromising illnesses. TB can usually be treated with a course of four standard, or Therapy#Lines of therapy, first-line, anti-TB drugs ...
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Mycobacterium Tuberculosis
''Mycobacterium tuberculosis'' (M. tb), also known as Koch's bacillus, is a species of pathogenic bacteria in the family Mycobacteriaceae and the causative agent of tuberculosis. First discovered in 1882 by Robert Koch, ''M. tuberculosis'' has an unusual, waxy coating on its cell surface primarily due to the presence of mycolic acid. This coating makes the cells impervious to Gram staining, and as a result, ''M. tuberculosis'' can appear weakly Gram-positive. Acid-fastness, Acid-fast stains such as Ziehl–Neelsen stain, Ziehl–Neelsen, or Fluorescence, fluorescent stains such as Auramine O, auramine are used instead to identify ''M. tuberculosis'' with a microscope. The physiology of ''M. tuberculosis'' is highly aerobic organism, aerobic and requires high levels of oxygen. Primarily a pathogen of the mammalian respiratory system, it infects the lungs. The most frequently used diagnostic methods for tuberculosis are the Mantoux test, tuberculin skin test, Acid-Fast Stain, aci ...
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Mycobacterium Tuberculosis Structural Genomics Consortium
The TB Structural Genomics Consortium (TBSGC) is a worldwide consortium of scientists developing a foundation for tuberculosis diagnosis and treatment by determining the three-dimensional structures of proteins from ''M. tuberculosis'' founded in 2000 as a part of the Protein Structure Initiative. The consortium seeks to solve structures of proteins that are of great interest to the TB biology community. A major goal of the consortium is to have a putative function for every ORF in the TB genome. __TOC__ Activities As of June 2006, 82 TB protein structures have been determined, 15 since January 1, 2006. The database of linked structural and functional information that has been constructed using this information can form a lasting basis for understanding ''M. tuberculosis'' pathogenesis and for structure-based drug design. As of June 2006, the TB Structural Genomics Consortium consists of 430 active members in 148 laboratories from 83 institutions across 15 countries. Consortium lab ...
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Escherichia Coli
''Escherichia coli'' ( )Wells, J. C. (2000) Longman Pronunciation Dictionary. Harlow ngland Pearson Education Ltd. is a gram-negative, facultative anaerobic, rod-shaped, coliform bacterium of the genus '' Escherichia'' that is commonly found in the lower intestine of warm-blooded organisms. Most ''E. coli'' strains are part of the normal microbiota of the gut, where they constitute about 0.1%, along with other facultative anaerobes. These bacteria are mostly harmless or even beneficial to humans. For example, some strains of ''E. coli'' benefit their hosts by producing vitamin K2 or by preventing the colonization of the intestine by harmful pathogenic bacteria. These mutually beneficial relationships between ''E. coli'' and humans are a type of mutualistic biological relationship—where both the humans and the ''E. coli'' are benefitting each other. ''E. coli'' is expelled into the environment within fecal matter. The bacterium grows massi ...
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Thermotoga
''Thermotoga'' is a genus of the phylum '' Thermotogota''. Members of ''Thermotoga'' are hyperthermophilic bacteria whose cell is wrapped in a unique sheath-like outer membrane, called a "toga". The members of the phylum stain Gram-negative as they possess a thin peptidoglycan in between two lipid bilayers, albeit both peculiar. The peptidoglycan is unusual as the crosslink is not only meso-diaminopimelate as occurs in Pseudomonadota, but D-lysine.All proteinogenic amino acids have the L- configuration; in peptidoglycan some amino acids with the D- configuration are present. Lysine is synthesised from meso-diaminopimelate by Diaminopimelate decarboxylase The species are anaerobes with varying degrees of oxygen tolerance. They are capable of reducing elemental sulphur (S0) to hydrogen sulphide. Whether thermophily is an innovation of the lineage or an ancestral trait is unclear and cannot be determined. The genome of '' Thermotoga maritima'' was sequenced in 1999, revealing se ...
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