HOME



picture info

Zinc Finger
A zinc finger is a small protein structural motif that is characterized by the coordination of one or more zinc ions (Zn2+) which stabilizes the fold. The term ''zinc finger'' was originally coined to describe the finger-like appearance of a hypothesized structure from the African clawed frog (''Xenopus laevis'') transcription factor IIIA. However, it has been found to encompass a wide variety of differing protein structures in eukaryotic cells. '' Xenopus laevis'' TFIIIA was originally demonstrated to contain zinc and require the metal for function in 1983, the first such reported zinc requirement for a gene regulatory protein followed soon thereafter by the Krüppel factor in ''Drosophila''. It often appears as a metal-binding domain in multi-domain proteins. Proteins that contain zinc fingers (zinc finger proteins) are classified into several different structural families. Unlike many other clearly defined supersecondary structures such as Greek keys or β hairpins, ...
[...More Info...]      
[...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]  


picture info

Zinc Finger Rendered
Zinc is a chemical element; it has Symbol (chemistry), symbol Zn and atomic number 30. It is a slightly brittle metal at room temperature and has a shiny-greyish appearance when oxidation is removed. It is the first element in group 12 element, group 12 (IIB) of the periodic table. In some respects, zinc is chemically similar to magnesium: both elements exhibit only one normal oxidation state (+2), and the Zn2+ and Mg2+ ions are of similar size. Zinc is the 24th most abundant Abundance of elements in Earth's crust, element in Earth's crust and has five stable isotopes. The most common zinc ore is sphalerite (zinc blende), a zinc sulfide mineral. The largest workable lodes are in Australia, Asia, and the United States. Zinc is refined by froth flotation of the ore, Roasting (metallurgy), roasting, and final extractive metallurgy, extraction using electricity (electrowinning). Zinc is an essential trace element for humans, animals, plants and for microorganisms and is necessary fo ...
[...More Info...]      
[...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]  


picture info

Ligands
In coordination chemistry, a ligand is an ion or molecule with a functional group that binds to a central metal atom to form a coordination complex. The bonding with the metal generally involves formal donation of one or more of the ligand's electron pairs, often through Lewis bases. The nature of metal–ligand bonding can range from covalent to ionic. Furthermore, the metal–ligand bond order can range from one to three. Ligands are viewed as Lewis bases, although rare cases are known to involve Lewis acidic "ligands". Metals and metalloids are bound to ligands in almost all circumstances, although gaseous "naked" metal ions can be generated in a high vacuum. Ligands in a complex dictate the reactivity of the central atom, including ligand substitution rates, the reactivity of the ligands themselves, and redox. Ligand selection requires critical consideration in many practical areas, including bioinorganic and medicinal chemistry, homogeneous catalysis, and environme ...
[...More Info...]      
[...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]  




Molecular Binding
Molecular binding is an attractive interaction between two molecules that results in a stable association in which the molecules are in close proximity to each other. It is formed when atoms or molecules bind together by sharing of electrons. It often, but not always, involves some chemical bonding. In some cases, the associations can be quite strong—for example, the protein streptavidin and the vitamin biotin have a dissociation constant (reflecting the ratio between bound and free biotin) on the order of 10−14—and so the reactions are effectively irreversible. The result of molecular binding is sometimes the formation of a molecular complex in which the attractive forces holding the components together are generally non-covalent, and thus are normally energetically weaker than covalent bonds. Molecular binding occurs in biological complexes (e.g., between pairs or sets of proteins, or between a protein and a small molecule ligand it binds) and also in abiologic chemic ...
[...More Info...]      
[...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]  


Protein Motif
In a chain-like biological molecule, such as a protein or nucleic acid, a structural motif is a common three-dimensional structure that appears in a variety of different, evolutionarily unrelated molecules. A structural motif does not have to be associated with a sequence motif; it can be represented by different and completely unrelated sequences in different proteins or RNA. In nucleic acids Depending upon the sequence and other conditions, nucleic acids can form a variety of structural motifs which is thought to have biological significance. ;Stem-loop: Stem-loop intramolecular base pairing is a pattern that can occur in single-stranded DNA or, more commonly, in RNA. The structure is also known as a hairpin or hairpin loop. It occurs when two regions of the same strand, usually complementary in nucleotide sequence when read in opposite directions, base-pair to form a double helix that ends in an unpaired loop. The resulting structure is a key building block of many ...
[...More Info...]      
[...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]  


picture info

Protein Domain
In molecular biology, a protein domain is a region of a protein's Peptide, polypeptide chain that is self-stabilizing and that Protein folding, folds independently from the rest. Each domain forms a compact folded Protein tertiary structure, three-dimensional structure. Many proteins consist of several domains, and a domain may appear in a variety of different proteins. Molecular evolution uses domains as building blocks and these may be recombined in different arrangements to create proteins with different functions. In general, domains vary in length from between about 50 amino acids up to 250 amino acids in length. The shortest domains, such as zinc fingers, are stabilized by metal ions or Disulfide bond, disulfide bridges. Domains often form functional units, such as the calcium-binding EF-hand, EF hand domain of calmodulin. Because they are independently stable, domains can be "swapped" by genetic engineering between one protein and another to make chimera (protein), chimeric ...
[...More Info...]      
[...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]  


John M
John is a common English name and surname: * John (given name) * John (surname) John may also refer to: New Testament Works * Gospel of John, a title often shortened to John * First Epistle of John, often shortened to 1 John * Second Epistle of John, often shortened to 2 John * Third Epistle of John, often shortened to 3 John People * John the Baptist (died ), regarded as a prophet and the forerunner of Jesus Christ * John the Apostle (died ), one of the twelve apostles of Jesus Christ * John the Evangelist, assigned author of the Fourth Gospel, once identified with the Apostle * John of Patmos, also known as John the Divine or John the Revelator, the author of the Book of Revelation, once identified with the Apostle * John the Presbyter, a figure either identified with or distinguished from the Apostle, the Evangelist and John of Patmos Other people with the given name Religious figures * John, father of Andrew the Apostle and Saint Peter * Pope John ( ...
[...More Info...]      
[...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]  


Demis Hassabis
Sir Demis Hassabis (born 27 July 1976) is a British artificial intelligence (AI) researcher, and entrepreneur. He is the chief executive officer and co-founder of Google DeepMind, and Isomorphic Labs, and a UK Government AI Adviser. In 2024, Hassabis and John M. Jumper were jointly awarded the Nobel Prize in Chemistry for their AI research contributions for protein structure prediction. Hassabis is a Fellow of the Royal Society, and has won many prestigious awards for his research work including the Breakthrough Prize, the Canada Gairdner International Award, and the Lasker Award. In 2017 he was appointed a CBE and listed in the Time 100 most influential people list. In 2024 he was knighted for services to AI, and was listed in the Time 100 again in 2025, this time featured in one of the five covers of the printed version. Early life and education Hassabis was born to Costas and Angela Hassabis. His father is Greek Cypriot and his mother is from Singapore. Demis grew up in ...
[...More Info...]      
[...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]  




David Baker (biochemist)
David Baker (born October 6, 1962) is an American biochemist and computational biology, computational biologist who has pioneered methods to Protein design, design proteins and protein structure prediction, predict their three-dimensional structures. He is the Henrietta and Aubrey Davis Endowed Professor in Biochemistry, an investigator with the Howard Hughes Medical Institute, and an adjunct professor of genome sciences, bioengineering, chemical engineering, computer science, and physics at the University of Washington. He was awarded the shared 2024 Nobel Prize in Chemistry for his work on computational protein design. Baker is a member of the United States National Academy of Sciences and the director of the University of Washington's Institute for Protein Design. He has co-founded more than a dozen biotechnology companies and was included in Time (magazine), ''Time'' magazine's inaugural list of the 100 Most Influential People in health in 2024. Biography Early life and ed ...
[...More Info...]      
[...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]  


picture info

Nobel Prize In Chemistry
The Nobel Prize in Chemistry () is awarded annually by the Royal Swedish Academy of Sciences to scientists in the various fields of chemistry. It is one of the five Nobel Prizes established by the will of Alfred Nobel in 1895, awarded for outstanding contributions in chemistry, physics, literature, peace, and physiology or medicine. This award is administered by the Nobel Foundation and awarded by the Royal Swedish Academy of Sciences on proposal of the Nobel Committee for Chemistry, which consists of five members elected by the Academy. The award is presented in Stockholm at an annual ceremony on December 10th, the anniversary of Nobel's death. The first Nobel Prize in Chemistry was awarded in 1901 to Jacobus Henricus van 't Hoff, of the Netherlands, "for his discovery of the laws of chemical dynamics and osmotic pressure in solutions". From 1901 to 2024, the award has been bestowed on a total of 195 individuals. The 2024 Nobel Prize in Chemistry was awarded to Demis Hassabis ...
[...More Info...]      
[...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]  


GC Box
In molecular biology, a GC box, also known as a GSG box, is a distinct pattern of nucleotides found in the promoter region of some eukaryotic genes. The GC box is upstream of the TATA box, and approximately 110 bases upstream from the transcription initiation site. It has a consensus sequence GGGCGG which is position-dependent and orientation-independent. The GC elements are bound by transcription factors and have similar functions to enhancers. Some known GC box-binding proteins include Sp1, Krox/Egr, Wilms' tumor, MIGI, and CREA. The GC box is commonly the binding site for zinc finger A zinc finger is a small protein structural motif that is characterized by the coordination of one or more zinc ions (Zn2+) which stabilizes the fold. The term ''zinc finger'' was originally coined to describe the finger-like appearance of a ... proteins. An alpha helix section of the protein corresponds with a major groove in the DNA. Zinc-fingers bind to triplet base pair sequences, with re ...
[...More Info...]      
[...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]  


picture info

Transcription Factor
In molecular biology, a transcription factor (TF) (or sequence-specific DNA-binding factor) is a protein that controls the rate of transcription (genetics), transcription of genetics, genetic information from DNA to messenger RNA, by binding to a specific DNA sequence. The function of TFs is to regulate—turn on and off—genes in order to make sure that they are Gene expression, expressed in the desired Cell (biology), cells at the right time and in the right amount throughout the life of the cell and the organism. Groups of TFs function in a coordinated fashion to direct cell division, cell growth, and cell death throughout life; cell migration and organization (body plan) during embryonic development; and intermittently in response to signals from outside the cell, such as a hormone. There are approximately 1600 TFs in the human genome. Transcription factors are members of the proteome as well as regulome. TFs work alone or with other proteins in a complex, by promoting (a ...
[...More Info...]      
[...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]