Literature DB >> 22236769

Conformation of poly-L-glutamate is independent of ionic strength.

Kan Xiong1, Lu Ma, Sanford A Asher.   

Abstract

CD and UV resonance Raman measurements surprisingly find that the charge screening of even 2 M concentrations of NaCl and KCl does not alter the unfolded PPII and 2.5(1)-helix conformations of poly-L-glutamate. These salts appear to be excluded from the region between the side chain charges and the peptide backbone. Furthermore, no direct ion pairing occurs between these salts and the side chain carboxylates. Copyright Â
© 2011 Elsevier B.V. All rights reserved.

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Year:  2011        PMID： 22236769      PMCID： PMC3288237          DOI： 10.1016/j.bpc.2011.11.002

Source DB:  PubMed          Journal:  Biophys Chem        ISSN： 0301-4622            Impact factor:   2.352


  22 in total

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Review 4.  The Hofmeister series: salt and solvent effects on interfacial phenomena.

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Review 5.  The Hofmeister effect and the behaviour of water at interfaces.

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6.  Charge density-dependent strength of hydration and biological structure.

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8.  Ion specificity in α-helical folding kinetics.

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9.  To switch or not to switch: the effects of potassium and sodium ions on alpha-poly-L-glutamate conformations in aqueous solutions.

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10.  Cation-specific interactions with carboxylate in amino acid and acetate aqueous solutions: X-ray absorption and ab initio calculations.

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  5 in total

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4.  Polyglutamine Solution-State Structural Propensity Is Repeat Length Dependent.

Authors:  Ryan S Jakubek; Riley J Workman; Stephen E White; Sanford A Asher
Journal:  J Phys Chem B       Date:  2019-05-01       Impact factor: 2.991

5.  Changes in the Local Conformational States Caused by Simple Na+ and K+ Ions in Polyelectrolyte Simulations: Comparison of Seven Force Fields with and without NBFIX and ECC Corrections.

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Journal:  Polymers (Basel)       Date:  2022-01-08       Impact factor: 4.329
  5 in total

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