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Titin
4UOW, 1BPV, 1G1C, 1NCT, 1NCU, 1TIT, 1TIU, 1TKI, 1TNM, 1TNN, 1WAA, 1YA5, 2A38, 2BK8, 2F8V, 2ILL, 2J8H, 2J8O, 2NZI, 2RQ8, 2WP3, 2WWK, 2WWM, 2Y9R, 3KNB, 3LCY, 3LPW, 3PUC, 3Q5O, 3QP3, 4C4K, 4JNW, 4O00, 4QEG, 5BS0IdentifiersAliases TTN, CMD1G, CMH9, CMPD4, EOMFC, HMERF, LGMD2J, MYLK5, TMD, titin, SALMYExternal IDs MGI: 98864 HomoloGene: 130650 GeneCards: TTN Gene
Gene
location (Human)Chr. Chromosome
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C-terminus
The C-terminus
C-terminus
(also known as the carboxyl-terminus, carboxy-terminus, C-terminal tail, C-terminal end, or COOH-terminus) is the end of an amino acid chain (protein or polypeptide), terminated by a free carboxyl group (-COOH). When the protein is translated from messenger RNA, it is created from N-terminus
N-terminus
to C-terminus. The convention for writing peptide sequences is to put the C-terminal end on the right and write the sequence from N- to C-terminus.Contents1 Chemistry 2 Function2.1 C-terminal retention signals 2.2 C-terminal modifications2.2.1 Prenylation 2.2.2 GPI anchors2.3 C-terminal domain3 See also 4 ReferencesChemistry[edit] Each amino acid has a carboxyl group and an amine group. Amino acids link to one another to form a chain by a dehydration reaction which joins the amine group of one amino acid to the carboxyl group of the next
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Protein Isoform
A protein isoform, or "protein variant"[1] is a member of a set of highly similar proteins that perform the same or similar biological roles. A set of protein isoforms may be formed from alternative splicings or other post-translational modifications of a single gene. Through RNA splicing
RNA splicing
mechanisms, mRNA has the ability to select different protein-coding segments (exons) of a gene, or even different parts of exons from RNA to form different mRNA sequences. Each unique sequence produces a specific form of a protein. A set of protein isoforms may also result from a set of closely related genes that evolved from a single gene in the past. The discovery of isoforms could explain the discrepancy between the small number of protein coding regions genes revealed by the human genome project and the large diversity of proteins seen in an organism: different proteins encoded by the same gene could increase the diversity of the proteome
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Denaturation (biochemistry)
Note 1: Modified from the definition given in ref.[1] Note 2: Denaturation can occur when proteins and nucleic acids are subjected to elevated temperature or to extremes of pH, or to nonphysiological concentrations of salt, organic solvents, urea, or other chemical agents. Note 3: An enzyme loses its catalytic activity when it is denaturized.[2]Denaturation is a process in which proteins or nucleic acids lose the quaternary structure, tertiary structure and secondary structure which is present in their native state, by application of some external stress or compound such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), radiation or heat.[3] If proteins in a living cell are denatured, this results in disruption of cell activity and possibly cell death. Protein
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Protein Folding
Protein
Protein
folding is the physical process by which a protein chain acquires its native 3-dimensional
3-dimensional
structure, a conformation that is usually biologically functional, in an expeditious and reproducible manner. It is the physical process by which a polypeptide folds into its characteristic and functional three-dimensional structure from random coil.[1] Each protein exists as an unfolded polypeptide or random coil when translated from a sequence of m RNA
RNA
to a linear chain of amino acids. This polypeptide lacks any stable (long-lasting) three-dimensional structure (the left hand side of the first figure). As the polypeptide chain is being synthesized by the ribosome, the linear chain begins to fold into its three dimensional structure. Folding begins to occur even during translation of the polypeptide chain
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Amino Acid
Amino acids
Amino acids
are organic compounds containing amine (-NH2) and carboxyl (-COOH) functional groups, along with a side chain (R group) specific to each amino acid.[1][2][3] The key elements of an amino acid are carbon (C), hydrogen (H), oxygen (O), and nitrogen (N), although other elements are found in the side chains of certain amino acids. About 500 naturally occurring amino acids are known (though only 20 appear in the genetic code) and can be classified in many ways.[4] They can be classified according to the core structural functional groups' locations as alpha- (α-), beta- (β-), gamma- (γ-) or delta- (δ-) amino acids; other categories relate to polarity, pH level, and side chain group type (aliphatic, acyclic, aromatic, containing hydroxyl or sulfur, etc.)
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Alternative Splicing
Alternative splicing, or differential splicing, is a regulated process during gene expression that results in a single gene coding for multiple proteins. In this process, particular exons of a gene may be included within or excluded from the final, processed messenger RNA (mRNA) produced from that gene.[1] Consequently, the proteins translated from alternatively spliced mRNAs will contain differences in their amino acid sequence and, often, in their biological functions (see Figure)
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Exon
An exon is any part of a gene that will encode a part of the final mature RNA
RNA
produced by that gene after introns have been removed by RNA
RNA
splicing. The term exon refers to both the DNA sequence within a gene and to the corresponding sequence in RNA
RNA
transcripts. In RNA splicing, introns are removed and exons are covalently joined to one another as part of generating the mature messenger RNA
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Gel Electrophoresis
Gel
Gel
electrophoresis is a method for separation and analysis of macromolecules (DNA, RNA
RNA
and proteins) and their fragments, based on their size and charge. It is used in clinical chemistry to separate proteins by charge and/or size (IEF agarose, essentially size independent) and in biochemistry and molecular biology to separate a mixed population of DNA
DNA
and RNA
RNA
fragments by length, to estimate the size of DNA
DNA
and RNA
RNA
fragments or to separate proteins by charge.[1] Nucleic acid
Nucleic acid
molecules are separated by applying an electric field to move the negatively charged molecules through a matrix of agarose or other substances. Shorter molecules move faster and migrate farther than longer ones because shorter molecules migrate more easily through the pores of the gel
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CDNA
In genetics, complementary DNA
DNA
(cDNA) is DNA
DNA
synthesized from a single stranded RNA
RNA
(e.g., messenger RNA
RNA
(mRNA) or microRNA) template in a reaction catalyzed by the enzyme reverse transcriptase. c DNA
DNA
is often used to clone eukaryotic genes in prokaryotes. When scientists want to express a specific protein in a cell that does not normally express that protein (i.e., heterologous expression), they will transfer the c DNA
DNA
that codes for the protein to the recipient cell
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Molecular Weight
Molecular mass or molecular weight is the mass of a molecule. It is calculated as the sum of the atomic weights of each constituent element multiplied by the number of atoms of that element in the molecular formula. The molecular mass of small to medium size molecules, measured by mass spectrometry, determines stoichiometry. For large molecules such as proteins, methods based on viscosity and light-scattering can be used to determine molecular mass when crystallographic data are not available.Contents1 Definitions 2 Determination2.1 Mass spectrometry 2.2 Hydrodynamic methods 2.3 Static light scattering3 See also 4 References 5 External linksDefinitions[edit] Both atomic and molecular masses are usually obtained relative to the mass of the isotope 12C (carbon 12), which by definition[1] is equal to 12
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Micrometre
The micrometre (International spelling as used by the International Bureau of Weights and Measures;[1] SI symbol: μm) or micrometer (American spelling), also commonly known as a micron, is an SI derived unit of length equaling 6994100000000000000♠1×10−6 metre (SI standard prefix "micro-" = 10−6); that is, one millionth of a metre (or one thousandth of a millimetre, 0.001 mm, or about 0.000039 inch).[1] The micrometre is a common unit of measurement for wavelengths of infrared radiation as well as sizes of biological cells and bacteria,[1] and for grading wool by the diameter of the fibres.[2] The width of a single human hair ranges from approximately 10 to 200 μm
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Isoelectric Point
The isoelectric point (pI, pH(I), IEP), is the pH at which a particular molecule carries no net electrical charge in the statistical mean. The standard nomenclature to represent the isoelectric point is pH(I),[1] although pI is also commonly seen,[2] and is used in this article for brevity. The net charge on the molecule is affected by pH of its surrounding environment and can become more positively or negatively charged due to the gain or loss, respectively, of protons (H+). Surfaces naturally charge to form a double layer. In the common case when the surface charge-determining ions are H+/OH−, the net surface charge is affected by the pH of the liquid in which the solid is submerged. The pI value can affect the solubility of a molecule at a given pH. Such molecules have minimum solubility in water or salt solutions at the pH that corresponds to their pI and often precipitate out of solution
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Chemical Formula
A chemical formula is a way of information about the chemical proportions of atoms that constitute a particular chemical compound or molecule, using chemical element symbols, numbers, and sometimes also other symbols, such as parentheses, dashes, brackets, commas and plus (+) and minus (−) signs. These are limited to a single typographic line of symbols, which may include subscripts and superscripts. A chemical formula is not a chemical name, and it contains no words. Although a chemical formula may imply certain simple chemical structures, it is not the same as a full chemical structural formula. Chemical formulas can fully specify the structure of only the simplest of molecules and chemical substances, and are generally more limited in power than are chemical names and structural formulas. The simplest types of chemical formulas are called empirical formulas, which use letters and numbers indicating the numerical proportions of atoms of each type
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Instability Index
The Instability index is a measure of proteins, used to determine whether it will be stable in a test tube. If the index is less than 40, then it is probably stable in the test tube. If it is greater (for example, enaptin) then it is probably not stable. References[edit]Guruprasad K, Reddy BV, Pandit MW (1990). "Correlation between stability of a protein and its dipeptide composition: a novel approach for predicting in vivo stability of a protein from its primary sequence". Protein
Protein
Eng. 4 (2): 155–61. doi:10.1093/protein/4.2.155. PMID 2075190. The instability index is also used to calculate risk in agriculture. External links[edit]ProtParam on ExPASy, computes the instability index of a protein sequence ProtParam documentationThis protein-related article is a stub. You can help by expanding it.v t eThis chemistry-related article is a stub
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In Vivo
Studies that are in vivo (Latin for "within the living"; often not italicized in English[1][2][3]) are those in which the effects of various biological entities are tested on whole, living organisms or cells, usually animals, including humans, and plants, as opposed to a tissue extract or dead organism. This is not to be confused with experiments done in vitro ("within the glass"), i.e., in a laboratory environment using test tubes, petri dishes, etc. Examples of investigations in vivo include: the pathogenesis of disease by comparing the effects of bacterial infection with the effects of purified bacterial toxins; the development of antibiotics, antiviral drugs, and new drugs generally; and new surgical procedures. Consequently, animal testing and clinical trials are major elements of in vivo research. In vivo testing is often employed over in vitro because it is better suited for observing the overall effects of an experiment on a living subject
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