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Top7
Top7 is an artificial 93-residue protein, classified as a '' de novo'' protein since it was designed by Brian Kuhlman and Gautam Dantas in David Baker's laboratory at the University of Washington to have a unique fold not found in nature. The protein was designed ''ab initio'' on a computer with the help of protein structure prediction algorithms. Determination of the high-resolution X-ray structure of the experimentally expressed and purified protein revealed that the structure (PDB ID1QYS was indeed very similar (1.2 Ã… RMSD) to the computer-designed model. The structure consists of two alpha helices packed on a five-stranded anti-parallel beta sheet. Top7 was featured as the RCSB Protein Data Bank's 'Molecule of the Month' in October 2005, and a superposition of the respective cores (residues 60-79) of its predicted and X-ray crystal structures are featured in the Rosetta@home Rosetta@home is a volunteer computing project researching protein structure prediction on the ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Top7 Superimp
Top7 is an artificial 93-residue protein, classified as a '' de novo'' protein since it was designed by Brian Kuhlman and Gautam Dantas in David Baker's laboratory at the University of Washington to have a unique fold not found in nature. The protein was designed ''ab initio'' on a computer with the help of protein structure prediction algorithms. Determination of the high-resolution X-ray structure of the experimentally expressed and purified protein revealed that the structure (PDB ID1QYS was indeed very similar (1.2 Ã… RMSD) to the computer-designed model. The structure consists of two alpha helices packed on a five-stranded anti-parallel beta sheet. Top7 was featured as the RCSB Protein Data Bank's 'Molecule of the Month' in October 2005, and a superposition of the respective cores (residues 60-79) of its predicted and X-ray crystal structures are featured in the Rosetta@home Rosetta@home is a volunteer computing project researching protein structure prediction on the Ber ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Top7
Top7 is an artificial 93-residue protein, classified as a '' de novo'' protein since it was designed by Brian Kuhlman and Gautam Dantas in David Baker's laboratory at the University of Washington to have a unique fold not found in nature. The protein was designed ''ab initio'' on a computer with the help of protein structure prediction algorithms. Determination of the high-resolution X-ray structure of the experimentally expressed and purified protein revealed that the structure (PDB ID1QYS was indeed very similar (1.2 Ã… RMSD) to the computer-designed model. The structure consists of two alpha helices packed on a five-stranded anti-parallel beta sheet. Top7 was featured as the RCSB Protein Data Bank's 'Molecule of the Month' in October 2005, and a superposition of the respective cores (residues 60-79) of its predicted and X-ray crystal structures are featured in the Rosetta@home Rosetta@home is a volunteer computing project researching protein structure prediction on the ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Design
Protein design is the rational design of new protein molecules to design novel activity, behavior, or purpose, and to advance basic understanding of protein function. Proteins can be designed from scratch (''de novo'' design) or by making calculated variants of a known protein structure and its sequence (termed ''protein redesign''). Rational protein design approaches make protein-sequence predictions that will fold to specific structures. These predicted sequences can then be validated experimentally through methods such as peptide synthesis, site-directed mutagenesis, or artificial gene synthesis. Rational protein design dates back to the mid-1970s. Recently, however, there were numerous examples of successful rational design of water-soluble and even transmembrane peptides and proteins, in part due to a better understanding of different factors contributing to protein structure stability and development of better computational methods. Overview and history The goal in ration ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Rosetta@home
Rosetta@home is a volunteer computing project researching protein structure prediction on the Berkeley Open Infrastructure for Network Computing (BOINC) platform, run by the Baker laboratory at the University of Washington. Rosetta@home aims to predict protein–protein docking and design new proteins with the help of about fifty-five thousand active volunteered computers processing at over 487,946 GigaFLOPS on average as of September 19, 2020. Foldit, a Rosetta@home videogame, aims to reach these goals with a crowdsourcing approach. Though much of the project is oriented toward basic research to improve the accuracy and robustness of proteomics methods, Rosetta@home also does applied research on malaria, Alzheimer's disease, and other pathologies. Like all BOINC projects, Rosetta@home uses idle computer processing resources from volunteers' computers to perform calculations on individual workunits. Completed results are sent to a central project server where they are validate ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
David Baker (biochemist)
__NOTOC__ David Baker (born October 6, 1962, in Seattle, Washington) is an American biochemist and computational biologist who has pioneered methods to predict and design the three-dimensional structures of proteins. He is the Henrietta and Aubrey Davis Endowed Professor in Biochemistry and an adjunct professor of Genome Sciences, Bioengineering, Chemical Engineering, Computer Science, and Physics at the University of Washington. He serves as the Director of the Rosetta Commons, a consortium of labs and researchers that develop biomolecular structure prediction and design software. The problem of protein structure prediction to which Baker has contributed significantly has now been solved completely by DeepMind using artificial intelligence. Baker is a Howard Hughes Medical Institute investigator and a member of the United States National Academy of Sciences. He is also the director of the University of Washington's Institute for Protein Design. Life Baker did his graduate work ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Root Mean Square Deviation (bioinformatics)
In bioinformatics, the root-mean-square deviation of atomic positions, or simply root-mean-square deviation (RMSD), is the measure of the average distance between the atoms (usually the backbone atoms) of superimposed proteins. Note that RMSD calculation can be applied to other, non-protein molecules, such as small organic molecules. In the study of globular protein conformations, one customarily measures the similarity in three-dimensional structure by the RMSD of the Cα atomic coordinates after optimal rigid body superposition. When a dynamical system fluctuates about some well-defined average position, the RMSD from the average over time can be referred to as the ''RMSF'' or root mean square fluctuation. The size of this fluctuation can be measured, for example using Mössbauer spectroscopy or nuclear magnetic resonance, and can provide important physical information. The Lindemann index is a method of placing the RMSF in the context of the parameters of the system. A wid ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Structural Alignment
Structural alignment attempts to establish homology between two or more polymer structures based on their shape and three-dimensional conformation. This process is usually applied to protein tertiary structures but can also be used for large RNA molecules. In contrast to simple structural superposition, where at least some equivalent residues of the two structures are known, structural alignment requires no ''a priori'' knowledge of equivalent positions. Structural alignment is a valuable tool for the comparison of proteins with low sequence similarity, where evolutionary relationships between proteins cannot be easily detected by standard sequence alignment techniques. Structural alignment can therefore be used to imply evolutionary relationships between proteins that share very little common sequence. However, caution should be used in using the results as evidence for shared evolutionary ancestry because of the possible confounding effects of convergent evolution by which mul ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Beta Sheet
The beta sheet, (β-sheet) (also β-pleated sheet) is a common motif of the regular protein secondary structure. Beta sheets consist of beta strands (β-strands) connected laterally by at least two or three backbone hydrogen bonds, forming a generally twisted, pleated sheet. A β-strand is a stretch of polypeptide chain typically 3 to 10 amino acids long with backbone in an extended conformation. The supramolecular association of β-sheets has been implicated in the formation of the fibrils and protein aggregates observed in amyloidosis, notably Alzheimer's disease. History The first β-sheet structure was proposed by William Astbury in the 1930s. He proposed the idea of hydrogen bonding between the peptide bonds of parallel or antiparallel extended β-strands. However, Astbury did not have the necessary data on the bond geometry of the amino acids in order to build accurate models, especially since he did not then know that the peptide bond was planar. A refined versi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Alpha Helix
The alpha helix (α-helix) is a common motif in the secondary structure of proteins and is a right hand-helix conformation in which every backbone N−H group hydrogen bonds to the backbone C=O group of the amino acid located four residues earlier along the protein sequence. The alpha helix is also called a classic Pauling–Corey–Branson α-helix. The name 3.613-helix is also used for this type of helix, denoting the average number of residues per helical turn, with 13 atoms being involved in the ring formed by the hydrogen bond. Among types of local structure in proteins, the α-helix is the most extreme and the most predictable from sequence, as well as the most prevalent. Discovery In the early 1930s, William Astbury showed that there were drastic changes in the X-ray fiber diffraction of moist wool or hair fibers upon significant stretching. The data suggested that the unstretched fibers had a coiled molecular structure with a characteristic repeat of ≈. Astb ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Structure Prediction
Protein structure prediction is the inference of the three-dimensional structure of a protein from its amino acid sequence—that is, the prediction of its secondary and tertiary structure from primary structure. Structure prediction is different from the inverse problem of protein design. Protein structure prediction is one of the most important goals pursued by computational biology; and it is important in medicine (for example, in drug design) and biotechnology (for example, in the design of novel enzymes). Starting in 1994, the performance of current methods is assessed biannually in the CASP experiment (Critical Assessment of Techniques for Protein Structure Prediction). A continuous evaluation of protein structure prediction web servers is performed by the community project CAMEO3D. Protein structure and terminology Proteins are chains of amino acids joined together by peptide bonds. Many conformations of this chain are possible due to the rotation of the main chain abou ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ångström
The angstromEntry "angstrom" in the Oxford online dictionary. Retrieved on 2019-03-02 from https://en.oxforddictionaries.com/definition/angstrom.Entry "angstrom" in the Merriam-Webster online dictionary. Retrieved on 2019-03-02 from https://www.merriam-webster.com/dictionary/angstrom. (, ; , ) or ångström is a metric unit of length equal to m; that is, one ten-billionth ( US) of a metre, a hundred-millionth of a centimetre,Entry "angstrom" in the Oxford English Dictionary, 2nd edition (1986). Retrieved on 2021-11-22 from https://www.oed.com/oed2/00008552. 0.1 nanometre, or 100 picometres. Its symbol is Å, a letter of the Swedish alphabet. The unit is named after the Swedish physicist Anders Jonas Ångström (1814–1874). The angstrom is often used in the natural sciences and technology to express sizes of atoms, molecules, microscopic biological structures, and lengths of chemical bonds, arrangement of atoms in crystals,Arturas Vailionis (2015):Geometry of Crystals Lect ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
X-ray Crystallography
X-ray crystallography is the experimental science determining the atomic and molecular structure of a crystal, in which the crystalline structure causes a beam of incident X-rays to diffract into many specific directions. By measuring the angles and intensities of these diffracted beams, a crystallographer can produce a three-dimensional picture of the density of electrons within the crystal. From this electron density, the mean positions of the atoms in the crystal can be determined, as well as their chemical bonds, their crystallographic disorder, and various other information. Since many materials can form crystals—such as salts, metals, minerals, semiconductors, as well as various inorganic, organic, and biological molecules—X-ray crystallography has been fundamental in the development of many scientific fields. In its first decades of use, this method determined the size of atoms, the lengths and types of chemical bonds, and the atomic-scale differences among various mat ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
