Salt effects in peptide solutions: theory and simulations

Marlow, Gail E.; Perkyns, John S.; Pettitt, B. Montgomery

doi:10.1021/cr00023a009

Cited by 38 publications

(22 citation statements)

References 65 publications

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“…The ions screen the charged side chains, reducing electrostatic interactions between neighboring parts of the protein. Molecular dynamics simulations, including explicit salt ions, have been performed previously for peptides and proteins using truncation schemes, 28,29 as well as the PME algorithm, 30,31 to treat electrostatic interactions. For a small WW domain (ϳ40 residues), it was found that explicit salt ions were essential to maintain the tertiary structure during a nanosecond molecular dynamics simulation utilizing the PME method.…”

Section: Introductionmentioning

confidence: 99%

Impact of Cl? and Na+ ions on simulated structure and dynamics of ?ARK1 PH domain

1999

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Section: Introductionmentioning

confidence: 99%

Impact of Cl? and Na+ ions on simulated structure and dynamics of ?ARK1 PH domain

1999

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“…These interactions between permanent charges of opposite sign have traditionally and most widely been studied for inorganic salts or simple acid ± base ion pairs. [4] Nature makes most efficient use of the same forces, for example with polyamines, [5] with nucleic acids, [6] with peptides, [7] peptide-or metal ± DNA associations, [8] and with proteins or enzymes. [9] Many applications, for instance in chromatography, also rely on ionic interactions.…”

Section: Introductionmentioning

confidence: 99%

Supramolecular Chemistry, Part 85[+] Flexibility, Association Constants, and Salt Effects in Organic Ion Pairs: How Single Bonds Affect Molecular Recognition

Hossain

Schneider

1999

Chem. Eur. J.

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Association free energies DG in water from NMR shift titrations with ten ion pairs from open-chain a,w-dianions and a,w-dications show a dependence on ionic strength that can be fitted to the Debye ± Hückel equation. In spite of the anisotropic nature of the ions, the D ± H coefficient m obtained in each case is close to the theoretical value m 4.07 for the dication/dianion combination. The DG values of the ten complexes and six literature values are all around 16 kJ mol À1 after extrapolation to ionic strength I 0.00, yielding a constant increment of 8 kJ mol À1 for each cation ± anion interaction. Although the number n of flexible single bonds in the ten complexes differs from 6 to 13, the difference between the strongest and the weakest complexes (DG À 16.3 and À 12.6 kJ mol À1, respectively) is surprisingly small. A fairly linear correlation between DG and n is observed, which yields an energetic disadvantage of only DDG 0.5 kJ mol À1for one single bond. This value is close to numbers obtained recently with similar hydrogen-bonded complexes in chloroform, and shows that until now the importance of conformational preorganization for effective molecular recognition has been overestimated.

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“…first-peak values are somewhat sensitive to the solute᎐ion potential parameters. Pettitt et al 23,24 and Marlow et al 24, 25 studied 1 M NaCl and 1 M CH COONa solutions near the zwitterionic 3 Ž . Ž .…”

Section: Solvation Free Energymentioning

confidence: 99%

Calculation of solvation free energy using RISM theory for peptide in salt solution

1998

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Salt effects in peptide solutions: theory and simulations

Cited by 38 publications

References 65 publications

Impact of Cl? and Na+ ions on simulated structure and dynamics of ?ARK1 PH domain

Impact of Cl? and Na+ ions on simulated structure and dynamics of ?ARK1 PH domain

Supramolecular Chemistry, Part 85[+] Flexibility, Association Constants, and Salt Effects in Organic Ion Pairs: How Single Bonds Affect Molecular Recognition

Calculation of solvation free energy using RISM theory for peptide in salt solution

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