Linkage of protonation and anion binding to the folding of Sac7d

McCrary, Bradford S.; Bedell, Jennifer L.; Edmondson, Stephen P.; Shriver, John W.

doi:10.1006/jmbi.1998.1500

Cited by 50 publications

(62 citation statements)

References 101 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The latter arises from the fact that the pK a value(s) of one or several groups on the ligand (peptide) or macromolecule (Ca 2ϩ -CaM) can change as a result of complex formation, as has been observed in a variety of other systems (45)(46)(47)(48)(49)(50). Hence, the change in the protonation upon binding can be characterized as the difference in the number of protons bound before and after complex formation, ⌬n ϩ .…”

Section: Resultsmentioning

confidence: 99%

Energetics of Target Peptide Binding by Calmodulin Reveals Different Modes of Binding

Brokx

López

Vogel

et al. 2001

Journal of Biological Chemistry

112

155

View full text Add to dashboard Cite

Understanding detailed molecular mechanisms that govern macromolecular interactions represents one of the major goals of structural biology. One of the important prerequisites for success in this line of research depends on the choice of an appropriate biological system. Calcium-dependent target recognition by calmodulin might be an ideal model system, because of its well characterized nature and its central role in cellular metabolism. Calmodulin (CaM) 1 is a small, acidic, eukaryotic Ca 2ϩ

show abstract

Section: Resultsmentioning

confidence: 99%

Energetics of Target Peptide Binding by Calmodulin Reveals Different Modes of Binding

Brokx

López

Vogel

et al. 2001

Journal of Biological Chemistry

112

155

View full text Add to dashboard Cite

show abstract

“…It is important to dissect (subtract) the energetic contribution of the linked reactions from the intrinsic binding reaction. Despite the fact that most researchers limit their efforts to determining only the observed parameters at certain experimental conditions, the intrinsic thermodynamic parameters of binding have been determined for various protein-ligand systems [60][61][62][63][64][65][66].…”

Section: Discussionmentioning

confidence: 99%

Thermodynamic characterization of human carbonic anhydrase VB stability and intrinsic binding of compounds

Kasiliauskaitė

Časaitė

Juozapaitienė

et al. 2015

J Therm Anal Calorim

View full text Add to dashboard Cite

The thermodynamics of low molecular weight synthetic sulfonamide inhibitor binding to carbonic anhydrase (CA) VB was determined by the isothermal titration calorimetry (ITC) and the fluorescent thermal shift assay (FTSA). ITC provided the enthalpic and entropic contributions to the binding affinity of ethoxzolamide to CA VB. FTSA is a high-throughput assay that measures protein thermal stabilization by added ligands. FTSA enabled determination of extremely high affinity of several compounds binding to CA VB. CA VB is one of two isoforms that are expressed in mitochondria, participate in carbon metabolism and pH homeostasis and are implicated in diseases such as obesity. Therefore CA VB is a drug target. Here a series of para-substituted tetrafluoro benzenesulfonamides were investigated as high affinity inhibitors of CA VB. Thermodynamic equilibrium binding measurements such as ITC and FTSA provide only the observed parameters. Dissection of binding-linked reactions is necessary to obtain the intrinsic parameters that in turn could be correlated with the chemical structure of the inhibitors. Intrinsic dissociation constants of the inhibitors were estimated and they reached 1 pM, one of the strongest binding reactions observed between any protein-ligand binding.

show abstract

“…Previous studies have shown that the B. subtilis P protein is intrinsically unstructured in the absence of PRNA or other anions, but it folds into a specific structure on addition of anions (Henkels et al 2001). The concentration of anion required to fold the P protein follows the anion binding series, indicating that specific ionic interactions are important for structure stabilization (Henkels et al 2001), as observed for acid-denatured Sac7d (McCrary et al 1998). To test whether the activation observed in the holoenzyme complex formation is due mainly to stabilization of the native fold of the P protein, we determined the dependence of the intraholoenzyme dissociation constant as a function of the ionic strength in the presence of 1 mM ATP.…”

Section: Rnase P Intraholoenzyme Interactionsmentioning

confidence: 90%

Ionic interactions between PRNA and P protein in Bacillus subtilis RNase P characterized using a magnetocapture-based assay

Day-Storms¹,

Niranjanakumari²,

Fierke³

2004

RNA

View full text Add to dashboard Cite

Ribonuclease P (RNase P) is a ribonucleoprotein complex that catalyzes the cleavage of the 5 end of precursor tRNA. To characterize the interface between the Bacillus subtilis RNA (PRNA) and protein (P protein) components, the intraholoenzyme K D is determined as a function of ionic strength using a magnetocapture-based assay. Three distinct phases are evident. At low ionic strength, the affinity of PRNA for P protein is enhanced as the ionic strength increases mainly due to stabilization of the PRNA structure by cations. Lithium substitution in lieu of potassium enhances the affinity at low ionic strength, whereas the addition of ATP, known to stabilize the structure of P protein, does not affect the affinity. At high ionic strength, the observed affinity decreases as the ionic strength increases, consistent with disruption of ionic interactions. These data indicate that three to four ions are released on formation of holoenzyme, reflecting the number of ion pairs that occur between the P protein and PRNA. At moderate ionic strength, the two effects balance so that the apparent K D is not dependent on the ionic strength. The K D between the catalytic domain (C domain) and P protein has a similar triphasic dependence on ionic strength. Furthermore, the intraholoenzyme K D is identical to or tighter than that of full-length PRNA, demonstrating that the P protein binds solely to the C domain. Finally, pre-tRNA asp (but not tRNA asp ) stabilizes the PRNA·P protein complex, as predicted by the direct interaction between the P protein and pre-tRNA leader.

show abstract

Linkage of protonation and anion binding to the folding of Sac7d

Cited by 50 publications

References 101 publications

Energetics of Target Peptide Binding by Calmodulin Reveals Different Modes of Binding

Energetics of Target Peptide Binding by Calmodulin Reveals Different Modes of Binding

Thermodynamic characterization of human carbonic anhydrase VB stability and intrinsic binding of compounds

Ionic interactions between PRNA and P protein in Bacillus subtilis RNase P characterized using a magnetocapture-based assay

Contact Info

Product

Resources

About