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Gene Section KIF14 (kinesin family member 14) Atlas of Genetics and Cytogenetics
Gene Section KIF14 (kinesin family member 14) Atlas of Genetics and Cytogenetics

... 274 aa kinesin motor domain containing an ATP-binding site (aa 447-454) which is involved in microtubule-dependent ATPase activity, and a microtubule binding site (aa 455-628) involved in ATP-dependent protein transport. The second is a 67 aa forkhead-associated (FHA) domain (aa 825-891) which has s ...
Chapter 5: What are the major types of organic molecules?
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... BIOL 1020 – CHAPTER 5 LECTURE NOTES C. proteins are polymers made of amino acid monomers linked together by peptide bonds 1. amino acids consist of a central or alpha carbon; bound to that carbon is a hydrogen atom, an amino group(-NH2), a carboxyl group (-COOH), and a variable side group (R group) ...
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... Corporation). Diffraction data for ADP- and ATP-bound complexes were collected with beamlines 19ID and 19BM in the Structural Biology Center at the Advanced Photon Source (Argonne, IL). The data were processed with MOSFLM (Leslie, 1992) or HKL2000 (Otwinowski and W. Minor, 1997). The crystals exhibi ...
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... Adapted from: Layman DK, USDA Food Composition Tables, J Nutr 133:261S-267S, 2003. Whey protein isolate offers more branched-chain amino acids and leucine than other typical protein ingredients. ...
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... Green Fluorescent Protein originates from the jellyfish Aequorea victoria. Unlike to other chromoproteins, that use separate cofactors, the chromophore in GFP is produced from three adjacend amino acids by an cyclization and oxidation step, and the only nececcity to do so is the presence of oxygen. ...
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... OR a) Briefly explain the importance of signal sequences in the secretion of proteins. b) “S. cerevisiae is a popular model organism in laboratory.” Explain why? c) How mating type switching occurs in S. cereisiae? Explain briefly mentioning the role of different proteins involved in this process. ...
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... • Radiation therapy works by damaging the DNA of cells. • The damage is caused by a photon, electron, proton, neutron, or ion beam directly or indirectly ionizing the atoms which make up the DNA chain. • Cells have mechanisms for repairing DNA damage, breaking the DNA on both strands proves to be th ...
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Cut and Paste Macromolecule Instructions

... glucoses together by cutting off and -H- from one molecule and an -OH- from another and taping the 2 molecules together forming a glyosidic bond. Give your disaccharide a name, bearing in mind that sugar names end in “-ose” (glucose, fructose) and write that name on the bottom of the molecule. 3. Th ...
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... along the I-helix, and phenylalanines 102, 481, and 483. The heme present is responsible for carrying out hydroxylation on substrates. If a drug can fit well into the binding site, it will be metabolized before it has done its job; if a drug does not fit easily, interactions may result because it wi ...
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... COLOR and LABEL the parts of a nucleotide --- sugar (5-sided)-green, phosphate group (round)yellow, and nitrogen base (6-sided)-blue. ATP used for cellular energy is a high energy nucleotide with three phosphate groups. Color code the ATP and LABEL THE PHOSPHATES. ...
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... 2. Most signal receptors are plasma membrane proteins • Most signal molecules are water-soluble and too large to pass through the plasma membrane. • They influence cell activities by binding to receptor proteins on the plasma membrane. • Binding leads to change in the shape or the receptor or to ag ...
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2 -1 -2 -1 1 2 K

... structure  One or more compact globular regions called domains  The tertiary structure associated with a domain region is also described as a protein fold Multi-domain  Proteins with polypeptide chains fold into several domains  Nearly half the known globular structures are multidomain, more tha ...
Supplemental Data
Supplemental Data

... incubating increasing amounts of wildtype or mutant Gal80 protein with a recombinant Gal4p derivative and a ...
< 1 ... 311 312 313 314 315 316 317 318 319 ... 520 >

Protein–protein interaction



Protein–protein interactions (PPIs) refer to physical contacts established between two or more proteins as a result of biochemical events and/or electrostatic forces.In fact, proteins are vital macromolecules, at both cellular and systemic levels, but they rarely act alone. Diverse essential molecular processes within a cell are carried out by molecular machines that are built from a large number of protein components organized by their PPIs. Indeed, these interactions are at the core of the entire interactomics system of any living cell and so, unsurprisingly, aberrant PPIs are on the basis of multiple diseases, such as Creutzfeld-Jacob, Alzheimer's disease, and cancer.PPIs have been studied from different perspectives: biochemistry, quantum chemistry, molecular dynamics, signal transduction, among others. All this information enables the creation of large protein interaction networks – similar to metabolic or genetic/epigenetic networks – that empower the current knowledge on biochemical cascades and disease pathogenesis, as well as provide putative new therapeutic targets.
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