When.com Web Search

Search results

  1. Results From The WOW.Com Content Network
  2. C-terminus - Wikipedia

    en.wikipedia.org/wiki/C-terminus

    The C-terminus (also known as the carboxyl-terminus, carboxy-terminus, C-terminal tail, carboxy 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 to C-terminus. The ...

  3. Membrane topology - Wikipedia

    en.wikipedia.org/wiki/Membrane_topology

    Group I proteins have the N terminus on the far side and C terminus on the cytosolic side. Group II proteins have the C terminus on the far side and N terminus in the cytosol. However final topology is not the only criterion for defining transmembrane protein groups, rather location of topogenic determinants and mechanism of assembly is ...

  4. Microtubule plus-end tracking protein - Wikipedia

    en.wikipedia.org/wiki/Microtubule_plus-end...

    The C-terminus however, sustains an alpha-helical coiled region which regulates parallel dimerization of EB monomers and comprises an acidic tail (attaining EEY/F motif) along with an EB homology domain (EBH). The EBH domain and or the EEY/F motif allow the EB proteins to physically interrelate with an array of +TIP in order to recruit them to ...

  5. Protein primary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_primary_structure

    The C-terminus can also be blocked (thus, neutralizing its negative charge) by amination. glycosyl phosphatidylinositol (GPI) attachment Glycosyl phosphatidylinositol (GPI) is a large, hydrophobic phospholipid prosthetic group that anchors proteins to cellular membranes .

  6. Integral membrane protein - Wikipedia

    en.wikipedia.org/wiki/Integral_membrane_protein

    Group I proteins have the N terminus on the far side and C terminus on the cytosolic side. Group II proteins have the C terminus on the far side and N terminus in the cytosol. Three-dimensional structures of ~160 different integral membrane proteins have been determined at atomic resolution by X-ray crystallography or nuclear magnetic resonance ...

  7. Microtubule-associated protein - Wikipedia

    en.wikipedia.org/wiki/Microtubule-associated_protein

    Usually, it is the C-terminal domain of the MAP that interacts with tubulin, while the N-terminal domain can bind with cellular vesicles, intermediate filaments or other microtubules. MAP-microtubule binding is regulated through MAP phosphorylation. This is accomplished through the function of the microtubule-affinity-regulating-kinase (MARK ...

  8. AOL Mail

    mail.aol.com

    Get AOL Mail for FREE! Manage your email like never before with travel, photo & document views. Personalize your inbox with themes & tabs. You've Got Mail!

  9. KDEL (amino acid sequence) - Wikipedia

    en.wikipedia.org/wiki/KDEL_(amino_acid_sequence)

    KDEL is a target peptide sequence in mammals and plants [1] [2] located on the C-terminal end of the amino acid structure of a protein.The KDEL sequence prevents a protein from being secreted from the endoplasmic reticulum (ER) and facilitates its return if it is accidentally exported.