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Istituto di scienza dell'alimentazione

Torna all'elenco Contributi in rivista anno 2017

Contributo in rivista

Tipo: Articolo in rivista

Titolo: Osmolyte-Like Stabilizing Effects of Low GdnHCl Concentrations on D-Glucose/D-Galactose-Binding Protein

Anno di pubblicazione: 2017

Autori: Fonin, Alexander V.; Golikova, Alexandra D.; Zvereva, Irina A.; D'Auria, Sabato; Staiano, Maria; Uversky, Vladimir N.; Kuznetsova, Irina M.; Turoverov, Konstantin K.

Affiliazioni autori: Russian Acad Sci; St Petersburg State Univ; CNR; Univ S Florida; Univ S Florida; Peter Great St Petersburg Polytech Univ

Autori CNR:

  • SABATO D'AURIA
  • MARIA STAIANO

Lingua: inglese

Abstract: The ability of D-glucose/D-galactose-binding protein (GGBP) to reversibly interact with its ligands, glucose and galactose, makes this protein an attractive candidate for sensing elements of glucose biosensors. This potential is largely responsible for attracting researchers to study the conformational properties of this protein. Previously, we showed that an increase in the fluorescence intensity of the fluorescent dye 6-bromoacetyl-2-dimetylaminonaphtalene (BADAN) is linked to the holo-form of the GGBP/H152C mutant in solutions containing sub-denaturing concentrations of guanidine hydrochloride (GdnHCl). It was hypothesized that low GdnHCl concentrations might lead to compaction of the protein, thereby facilitating ligand binding. In this work, we utilize BADAN fluorescence spectroscopy, intrinsic protein UV fluorescence spectroscopy, and isothermal titration calorimetry (ITC) to show that the sub-denaturing GdnHCl concentrations possess osmolyte-like stabilizing effects on the structural dynamics, conformational stability, and functional activity of GGBP/H152C and the wild type of this protein (wtGGBP). Our data are consistent with the model where low GdnHCl concentrations promote a shift in the dynamic distribution of the protein molecules toward a conformational ensemble enriched in molecules with a tighter structure and a more closed conformation. This promotes the increase in the configurational complementarity between the protein and glucose molecules that leads to the increase in glucose affinity in both GGBP/H152C and wtGGBP.

Lingua abstract: inglese

Pagine totali: 20

Rivista:

International journal of molecular sciences MDPI Center,
Paese di pubblicazione:
Lingua: inglese
ISSN: 1422-0067

Numero volume: 18

Numero fascicolo: 9

DOI: 10.3390/ijms18092008

Stato della pubblicazione: Published version

Indicizzato da: ISI Web of Science (WOS) [000411963800187]

Parole chiave:

  • D-glucose
  • D-galactose-binding protein
  • guanidine hydrochloride
  • osmolyte-like stabilizing effect
  • fluorescent label BADAN
  • protein conformers
  • protein function
  • conformational ensemble

Strutture CNR:

 
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