Journal ArticleDOI
Isoelectric points of proteins: Theoretical determination
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TLDR
Three methods for calculating the isoelectric points (pI) of proteins, provided that their amino acid compositions are known, are described.About:
This article is published in Analytical Biochemistry.The article was published on 1989-06-01. It has received 147 citations till now. The article focuses on the topics: Isoelectric point.read more
Citations
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Solution conformations and aggregational properties of synthetic amyloid beta-peptides of Alzheimer's disease. Analysis of circular dichroism spectra.
TL;DR: Differences between the solution conformations of the beta-(1-39) and beta-1-42 peptides suggests that the last 3 C-terminal amino acids are crucial to amyloid deposition, and suggests that beta-peptide is not an intrinsically insoluble peptide.
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Influence of Matrix Solution Conditions on the MALDI-MS Analysis of Peptides and Proteins
Steven L. Cohen,Brian T. Chait +1 more
TL;DR: Results indicate that there is a reverse-phase chromatographic-like dimension in the sample-matrix preparation procedures that can be exploited to optimize the analysis of MALDI mass spectra.
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IPC – Isoelectric Point Calculator
TL;DR: This article presents the Isoelectric Point Calculator (IPC), a web service and a standalone program for the accurate estimation of protein and peptide pI using different sets of dissociation constant (pKa) values, including two new computationally optimized pKa sets.
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Purification and primary structure of pediocin PA-1 produced by Pediococcus acidilactici PAC-1.0.
TL;DR: The purified product exhibited antibacterial activity against several gram-positive bacterial strains, including the food pathogen Listeria monocytogenes, and the amino acid sequence and arrangement of the disulfide bonds were determined.
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The effect of net charge on the solubility, activity, and stability of ribonuclease Sa
TL;DR: The pH of minimum solubility varies with the pI of the protein, but that the pH of maximum activity and the pHOf maximum stability do not, and pI values estimated using pK values based on model compound data can be in error.
References
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Journal ArticleDOI
High resolution two-dimensional electrophoresis of proteins.
TL;DR: This technique provides a method for estimation of the number of proteins made by any biological system and can resolve proteins differing in a single charge and consequently can be used in the analysis of in vivo modifications resulting in a change in charge.
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Isoelectric points and molecular weights of proteins.
TL;DR: Proteins with known isoelectric points (pI), as determined by isoeLECTric focusing, have been tabulated and, in the case of proteins displaying microheterogeneity, the major components have been indicated.
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Electrostatic effects in proteins
TL;DR: The present study presents a meta-analysis of protein structure and activity in the context of a long-range electric field, which highlights the importance of knowing the carrier and removal status of the carrier molecule.
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Chromatofocusing: Isoelectric focusing on ion-exchange columns : I. General Principles
L.A.A.E. Sluyterman,O. Elgersma +1 more
TL;DR: In this article, the width of the protein bands, taking into account axial diffusion and axial dispersion by non-uniformity of flow and for the pH at which proteins are expected to emerge from the column, are derived.
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On the calculation of electrostatic interactions in proteins
TL;DR: A classical treatment of electrostatic interactions in proteins is presented, treated as a region of low dielectric constant with spherical charges embedded within it, surrounded by an aqueous solvent of high dielectic constant, which may contain a simple electrolyte.