ArticleThe protein journal2011
Influence of pK(a) shifts on the calculated dipole moments of proteins.
Article in The protein journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed, 4 citations in OpenAlex.
- Electric charge and salting in/out effects on glucagon's dipole moments and polarizabilities using the GruPol database.Acta crystallographica Section B, Structural science, crystal engineering and materials · 2025Article
- Unveiling GruPol: Predicting Electric and Electrostatic Properties of Macromolecules via the Building Block Approach.The journal of physical chemistry. B · 2024Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The protein dipole moment is a low-resolution parameter that characterizes the second-order charge organization of a biomolecule. Theoretical approaches to calculate protein dipole moments rely on pK(a) values, which are either computed individually for each ionizable residue or obtained from model compounds. The influence of pK(a) shifts are evaluated first by comparing calculated and measured dipole moments of β-lactoglobulin. Second, calculations are made on a dataset of 66 proteins from the Protein Data Bank, and average differences are determined between dipole moments calculated with model pK(a)s, pK(a)s derived using a Poisson-Boltzmann approach, and empirically-calculated pK(a)s. Dipole moment predictions that neglect pK(a) shifts are consistently larger than predictions in which they are included. The importance of pK(a) shifts are observed to vary with protein size, internal permittivity, and solution pH.
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Registered trials
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