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NMR assignment of intrinsically disordered self-processing module of the FrpC protein of Neisseria meningitidis

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F15%3A00085528" target="_blank" >RIV/00216224:14740/15:00085528 - isvavai.cz</a>

  • Alternative codes found

    RIV/61388971:_____/15:00452973

  • Result on the web

    <a href="http://download.springer.com/static/pdf/605/art%253A10.1007%252Fs12104-015-9625-z.pdf?originUrl=http%3A%2F%2Flink.springer.com%2Farticle%2F10.1007%2Fs12104-015-9625-z&token2=exp=1451977460~acl=%2Fstatic%2Fpdf%2F605%2Fart%25253A10.1007%25252Fs12104-015-96" target="_blank" >http://download.springer.com/static/pdf/605/art%253A10.1007%252Fs12104-015-9625-z.pdf?originUrl=http%3A%2F%2Flink.springer.com%2Farticle%2F10.1007%2Fs12104-015-9625-z&token2=exp=1451977460~acl=%2Fstatic%2Fpdf%2F605%2Fart%25253A10.1007%25252Fs12104-015-96</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1007/s12104-015-9625-z" target="_blank" >10.1007/s12104-015-9625-z</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    NMR assignment of intrinsically disordered self-processing module of the FrpC protein of Neisseria meningitidis

  • Original language description

    The self-processing module (SPM) is an internal segment of the FrpC protein (P415-F591) secreted by the pathogenic Gram-negative bacterium Neisseria meningitidis during meningococcal infection of human upper respiratory tract. SPM mediates 'protein trans-splicing', a unique natural mechanism for editing of proteins, which involves a calcium-dependent autocatalytic cleavage of the peptide bond between D414 and P415 and covalent linkage of the cleaved fragment through its carboxy-terminal group of D414 to-amino group of lysine residue within a neighboring polypeptide chain. We present an NMR resonance assignment of the calcium-free SPM, which displays characteristic features of intrinsically disordered proteins. Non-uniformly sampled 5D HN(CA)CONH, 4D HCBCACON, and HCBCANCO spectra were recorded to resolve poorly dispersed resonance frequencies of the disordered protein and 91 % of SPM residues were unambiguously assigned.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    EE - Microbiology, virology

  • OECD FORD branch

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2015

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Biomolecular NMr Assignments

  • ISSN

    1874-2718

  • e-ISSN

  • Volume of the periodical

    9

  • Issue of the periodical within the volume

    2

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    6

  • Pages from-to

    435-440

  • UT code for WoS article

    000361440100046

  • EID of the result in the Scopus database