SwePub
Tyck till om SwePub Sök här!
Sök i SwePub databas

  Utökad sökning

Träfflista för sökning "WFRF:(Head Gordon Teresa) "

Sökning: WFRF:(Head Gordon Teresa)

  • Resultat 1-2 av 2
Sortera/gruppera träfflistan
   
NumreringReferensOmslagsbildHitta
1.
  • Lazar, Tamas, et al. (författare)
  • PED in 2021 : A major update of the protein ensemble database for intrinsically disordered proteins
  • 2021
  • Ingår i: Nucleic Acids Research. - : Oxford University Press (OUP). - 0305-1048 .- 1362-4962. ; 49:D1, s. 404-411
  • Tidskriftsartikel (refereegranskat)abstract
    • The Protein Ensemble Database (PED) (https://proteinensemble.org), which holds structural ensembles of intrinsically disordered proteins (IDPs), has been significantly updated and upgraded since its last release in 2016. The new version, PED 4.0, has been completely redesigned and reimplemented with cutting-edge technology and now holds about six times more data (162 versus 24 entries and 242 versus 60 structural ensembles) and a broader representation of state of the art ensemble generation methods than the previous version. The database has a completely renewed graphical interface with an interactive feature viewer for region-based annotations, and provides a series of descriptors of the qualitative and quantitative properties of the ensembles. High quality of the data is guaranteed by a new submission process, which combines both automatic and manual evaluation steps. A team of biocurators integrate structured metadata describing the ensemble generation methodology, experimental constraints and conditions. A new search engine allows the user to build advanced queries and search all entry fields including cross-references to IDP-related resources such as DisProt, MobiDB, BMRB and SASBDB. We expect that the renewed PED will be useful for researchers interested in the atomic-level understanding of IDP function, and promote the rational, structure-based design of IDP-targeting drugs.
  •  
2.
  • Li, Wan-Lu, et al. (författare)
  • How thermal fluctuations influence the function of the FeMo cofactor in nitrogenase enzymes
  • 2023
  • Ingår i: CHEM CATALYSIS. - : Elsevier BV. - 2667-1093. ; 3:7
  • Tidskriftsartikel (refereegranskat)abstract
    • The catalytic mechanism of N2 fixation by nitrogenase remains unre-solved in how the strong N=N bond is activated and why the reduc-tive elimination of H2 is required. Here, we use density functional theory and physiologically relevant thermal simulations to elucidate the mechanism of the complete nitrogenase catalytic cycle. Over the accumulation of four reducing equivalents, we find that protons and electrons transfer to the FeMo cofactor to weaken and break its bridge Fe-S bond, leading to temporary H2S formation that exposes the Fe sites to weakly bind N2. Remarkably, we find that subsequent H2 formation is responsible for chemical activation to an N=N dou-ble bond accompanied by a low barrier for H2 release. We empha-size that finite temperature effects smooth out mechanistic differ-ences between DFT functionals observed at 0 K, thus leading to a consistent understanding as to why H formation is an obligatory step in N2 adsorption and activation.
  •  
Skapa referenser, mejla, bekava och länka
  • Resultat 1-2 av 2

Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.

 
pil uppåt Stäng

Kopiera och spara länken för att återkomma till aktuell vy