Studies on the relationship between structure and electrophoretic mobility of α-helical and β-sheet peptides using capillary zone electrophoresis

Sitaram, Balvant R.; Keah, Hooi-Hong; Hearn, Milton Thomas William

doi:10.1016/s0021-9673(99)00768-2

Cited by 27 publications

(15 citation statements)

References 27 publications

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“…In generating this particular conformation, the SSM parameters were set to RRRRRHHHHHHHJRR, or R 5 H 7 JR 2 for short. As discussed elsewhere [14], the central seven residues, DDKNWDR, are likely to be in a helical conformation…”

Section: Methods (Peptide Modeling)mentioning

confidence: 85%

“…As a final illustrative example of how our modeling methodology can be applied to electrophoretic mobility data in an attempt to extract information about group pK a s and conformation, several peptides studied by Sitaram et al [14] shall be examined. The set of peptides in this study were chosen on the basis of their propensity to adopt specific secondary structures in solution.…”

Section: Resultsmentioning

confidence: 99%

“…Using the numbering scheme of ref. [14], we shall consider #4 DDA-LYDDKNWDRAPQ, #14 DDALYDDKNWDRAPQRCYYQ, and #15 which is identical to #14 except that the C-terminal is amidated (and can bear no charge). The experimental mobilities of these three peptides is 0.72, 1.17, and between them is most likely due to the protonation state of the C-terminal in #14.…”

Section: Resultsmentioning

confidence: 99%

“…1 is a sample conformation of the 15 subunit peptide, DDALYDDKNWDRAPQ, which shall be called #4 following the convention of ref. [14]. In generating this particular conformation, the SSM parameters were set to RRRRRHHHHHHHJRR, or R 5 H 7 JR 2 for short.…”

Section: Methods (Peptide Modeling)mentioning

confidence: 99%

“…In the present work, we apply the "bead model" method [37 -39] in modeling the free solution electrophoresis of a number of specific peptides [12,14] in order to illustrate how this approach can be used to estimate the pK a s of specific side groups and also what the influence of conformation has on mobility. This structurebased methodology is grounded on fundamental electrohydrodynamic theory.…”

Section: Introductionmentioning

confidence: 99%

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Using electrophoretic mobility and bead modeling to characterize the charge and secondary structure of peptides

Pei

Yao

Allison³

2008

J of Separation Science

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Using a modeling methodology developed in our laboratory previously, the free solution electrophoretic mobilities of several peptides are examined to see what they can tell us about: (i) the pK(a)s of specific side groups, and (ii) possible secondary structure. Modeling is first applied to mobility versus pH data of several small peptides (Messana, I. et al., J. Chromatogr. B 1997, 699, 149) where the only adjustable parameter associated with the charge state of the peptide is the pK(a )of the C-terminal. In addition to examining this parameter, the question of possible secondary structure is addressed. For two of the peptides considered, GGNA and GGQA, it is possible to account for the observed mobilities using "random" models with little restriction on the allowed range of Phi-Psi angles. For GGRA and RPPGF, "compact" models (possibly involving an I-turn) must be used to match modeling mobilities with experiment. Finally, three more complicated peptides ranging in size from 15 to 20 amino acids are also examined and characterized (Sitaram, B. R. et al., J. Chromatogr. A 1999, 857, 263). Here also, we find evidence of I-turns or some other "compact" structure in two of the three peptides examined.

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Section: Methods (Peptide Modeling)mentioning

confidence: 85%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Methods (Peptide Modeling)mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Using electrophoretic mobility and bead modeling to characterize the charge and secondary structure of peptides

Pei

Yao

Allison³

2008

J of Separation Science

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Recent advances in capillary electrophoresis of peptides

Kašička

2001

Electrophoresis

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The article gives a comprehensive review on the recent developments in the applications of high-performance capillary electromigration methods, including zone electrophoresis, isotachophoresis, isoelectric focusing, affinity electrophoresis, electrokinetic chromatography and electrochromatography, to analysis, preparation and physicochemical characterization of peptides. The article presents new approaches to the theoretical description and experimental verification of electromigration behavior of peptides, and covers the methodological aspects of capillary electroseparations of peptides, such as strategy and rules for the rational selection of separation mode and experimental conditions, sample treatment, suppression of peptide adsorption to the inner capillary wall, new developments in individual separation modes and new designs of detection systems. Several types of applications of capillary electromigration methods to peptide analysis are presented: conventional qualitative and quantitative analysis for determination of purity, determination in biomatrices, monitoring of physical and chemical changes and enzymatic conversions, amino acid and sequence analysis and peptide mapping of proteins. Some examples of micropreparative peptide separations are given and capabilities of capillary electromigration techniques to provide important physicochemical characteristics of peptides are demonstrated.

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Capillary electrophoresis of proteins 1999-2001

Dolnı́k¹,

Hutterer²

2001

Electrophoresis

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This review article with 223 references describes recent developments in capillary electrophoresis (CE) of proteins and covers papers published during last two years, from the previous review (V. Dolnik, Electrophoresis 1999, 20, 3106-3115) through Spring 2001. It describes the topics related to CE of proteins including modeling of the electrophoretic properties of proteins, sample pretreatment, wall coatings, improving selectivity, detection, special electrophoretic techniques, and applications.

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Studies on the relationship between structure and electrophoretic mobility of α-helical and β-sheet peptides using capillary zone electrophoresis

Cited by 27 publications

References 27 publications

Using electrophoretic mobility and bead modeling to characterize the charge and secondary structure of peptides

Using electrophoretic mobility and bead modeling to characterize the charge and secondary structure of peptides

Recent advances in capillary electrophoresis of peptides

Capillary electrophoresis of proteins 1999-2001

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