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  2. Protein primary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_primary_structure

    Protein primary structure is the linear sequence of amino acids in a peptide or protein. [1] By convention, the primary structure of a protein is reported starting from the amino-terminal (N) end to the carboxyl-terminal (C) end. Protein biosynthesis is most commonly performed by ribosomes in cells. Peptides can also be synthesized in the ...

  3. Glycerophospholipid - Wikipedia

    en.wikipedia.org/wiki/Glycerophospholipid

    Cells will use this phosphatidylserine to enter cells via apoptotic mimicry. The structure of this lipid differs in plants and animals, regarding fatty acid composition. In addition, phosphatidylserine plays an important role in the human brain content, as it makes up 13–15% of the phospholipids in the human cerebral cortex.

  4. Phosphatidylserine - Wikipedia

    en.wikipedia.org/wiki/Phosphatidylserine

    Phosphatidylserine (PS) is the major acidic phospholipid class that accounts for 13–15% of the phospholipids in the human cerebral cortex. [7] In the plasma membrane, PS is localized exclusively in the cytoplasmic leaflet where it forms part of protein docking sites necessary for the activation of several key signaling pathways.

  5. Dephosphorylation - Wikipedia

    en.wikipedia.org/wiki/Dephosphorylation

    During the synthesis of proteins, polypeptide chains, which are created by ribosomes translating mRNA, must be processed before assuming a mature conformation. The dephosphorylation of proteins is a mechanism for modifying behavior of a protein, often by activating or inactivating an enzyme. Components of the protein synthesis apparatus also ...

  6. Eukaryotic translation termination factor 1 - Wikipedia

    en.wikipedia.org/wiki/Eukaryotic_translation...

    Once in position, the water molecule acts as a nucleophile, and attacks the carbonyl group of the ester bond between the nascent protein and the tRNA. The hydrolysis of the ester bond causes the release of the nascent protein and the disassembly of the ribosome and termination complex. [37] Hydrolysis of ester bond to release nascent protein [37]

  7. Ubiquitin - Wikipedia

    en.wikipedia.org/wiki/Ubiquitin

    Ubiquitin is a small (8.6 kDa) regulatory protein found in most tissues of eukaryotic organisms, i.e., it is found ubiquitously. It was discovered in 1975 [1] by Gideon Goldstein and further characterized throughout the late 1970s and 1980s. [2] Four genes in the human genome code for ubiquitin: UBB, UBC, UBA52 and RPS27A. [3]

  8. Aster (cell biology) - Wikipedia

    en.wikipedia.org/wiki/Aster_(cell_biology)

    This diagram depicts the organization of a typical mitotic spindle found in animal cells. Chromosomes are attached to kinetochore microtubules via a multiprotein complex called the kinetochore. Polar microtubules interdigitate at the spindle midzone and push the spindle poles apart via motor proteins.

  9. Phosphodiester bond - Wikipedia

    en.wikipedia.org/wiki/Phosphodiester_bond

    Specifically, it is the phosphodiester bonds that link the 3' carbon atom of one sugar molecule and the 5' carbon atom of another (hence the name 3', 5' phosphodiester linkage used with reference to this kind of bond in DNA and RNA chains). [3] The involved saccharide groups are deoxyribose in DNA and ribose in RNA.

  1. Related searches ester bond proteins are found in small cell division called the primary

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    protein primary structure wikipediapolypeptides primary structure