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Literature DB >> 12496071

Residual charge interactions in unfolded staphylococcal nuclease can be explained by the Gaussian-chain model.

Abstract

The discrepancy of the pH dependence of the unfolding free energy for staphylococcal nuclease from what is expected from an idealized model for the unfolded state is accounted for by the recently developed Gaussian-chain model. Residual electrostatic effects in the unfolded state are attributed to nonspecific interactions dominated by charges close along the sequence. The dominance of nonspecific local interactions appears to be supported by some experimental evidence.

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Year: 2002 PMID： 12496071 PMCID： PMC1302379 DOI： 10.1016/S0006-3495(02)75304-6

Source DB: PubMed Journal: Biophys J ISSN： 0006-3495 Impact factor: 4.033

35 in total

1. pKa values and the pH dependent stability of the N-terminal domain of L9 as probes of electrostatic interactions in the denatured state. Differentiation between local and nonlocal interactions.

Authors: B Kuhlman; D L Luisi; P Young; D P Raleigh
Journal: Biochemistry Date: 1999-04-13 Impact factor: 3.162

2. Structural and dynamical properties of a denatured protein. Heteronuclear 3D NMR experiments and theoretical simulations of lysozyme in 8 M urea.

Authors: H Schwalbe; K M Fiebig; M Buck; J A Jones; S B Grimshaw; A Spencer; S J Glaser; L J Smith; C M Dobson
Journal: Biochemistry Date: 1997-07-22 Impact factor: 3.162

3. Perturbed pKA-values in the denatured states of proteins.

Authors: Y J Tan; M Oliveberg; B Davis; A R Fersht
Journal: J Mol Biol Date: 1995-12-15 Impact factor: 5.469

4. Characterization of long-range structure in the denatured state of staphylococcal nuclease. II. Distance restraints from paramagnetic relaxation and calculation of an ensemble of structures.

Authors: J R Gillespie; D Shortle
Journal: J Mol Biol Date: 1997-04-25 Impact factor: 5.469

5. Modeling of protein conformational fluctuations in pKa predictions.

Authors: H X Zhou; M Vijayakumar
Journal: J Mol Biol Date: 1997-04-11 Impact factor: 5.469

Review 6. The denatured state (the other half of the folding equation) and its role in protein stability.

Authors: D Shortle
Journal: FASEB J Date: 1996-01 Impact factor: 5.191

7. NMR determination of residual structure in a urea-denatured protein, the 434-repressor.

Authors: D Neri; M Billeter; G Wider; K Wüthrich
Journal: Science Date: 1992-09-11 Impact factor: 47.728

8. Structural characterization of the FK506 binding protein unfolded in urea and guanidine hydrochloride.

Authors: T M Logan; Y Thériault; S W Fesik
Journal: J Mol Biol Date: 1994-02-18 Impact factor: 5.469

9. Contributions of the ionizable amino acids to the stability of staphylococcal nuclease.

Authors: A K Meeker; B Garcia-Moreno; D Shortle
Journal: Biochemistry Date: 1996-05-21 Impact factor: 3.162

10. pKA values of carboxyl groups in the native and denatured states of barnase: the pKA values of the denatured state are on average 0.4 units lower than those of model compounds.

Authors: M Oliveberg; V L Arcus; A R Fersht
Journal: Biochemistry Date: 1995-07-25 Impact factor: 3.162

8 in total

Residual charge interactions in unfolded staphylococcal nuclease can be explained by the Gaussian-chain model.

1. pKa values and the pH dependent stability of the N-terminal domain of L9 as probes of electrostatic interactions in the denatured state. Differentiation between local and nonlocal interactions.

2. Structural and dynamical properties of a denatured protein. Heteronuclear 3D NMR experiments and theoretical simulations of lysozyme in 8 M urea.

3. Perturbed pKA-values in the denatured states of proteins.

4. Characterization of long-range structure in the denatured state of staphylococcal nuclease. II. Distance restraints from paramagnetic relaxation and calculation of an ensemble of structures.

5. Modeling of protein conformational fluctuations in pKa predictions.

Review 6. The denatured state (the other half of the folding equation) and its role in protein stability.

7. NMR determination of residual structure in a urea-denatured protein, the 434-repressor.

8. Structural characterization of the FK506 binding protein unfolded in urea and guanidine hydrochloride.

9. Contributions of the ionizable amino acids to the stability of staphylococcal nuclease.

10. pKA values of carboxyl groups in the native and denatured states of barnase: the pKA values of the denatured state are on average 0.4 units lower than those of model compounds.

1. Site-specific contributions to the pH dependence of protein stability.

2. Electrostatic contributions to the stability of a thermophilic cold shock protein.

3. pK(a) values for the unfolded state under native conditions explain the pH-dependent stability of PGB1.

4. pK(a) values for side-chain carboxyl groups of a PGB1 variant explain salt and pH-dependent stability.

5. NMR determination of pKa values in α-synuclein.

6. Electrostatic effects in unfolded staphylococcal nuclease.

7. Electrostatic effects on the folding stability of FKBP12.

Review 8. Electrostatic Interactions in Protein Structure, Folding, Binding, and Condensation.