Comparison of protein electrostatic potential along the catalytic triad of serine proteinases

Ángyán, János G.; Náray‐Szabó, Gábor

doi:10.1016/0022-5193(83)90291-6

Cited by 40 publications

(6 citation statements)

References 18 publications

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“…Matrix Isolation Fourier Transform Infrared Study of the Products of the Reaction between CIO and N02 J. P. Burrows,* D. W. T. Griffith, G. K. Moortgat, and G. S. Tyndall Max-Planck-Instituí f. Chemie, D-6500 Mainz, F.R.G. (Received: September 17, 1984) Matrix isolation FTIR and UV absorption spectroscopy have been used to study the products of the reaction between CIO and N02, a reaction of importance in the stratosphere. The technique allows both quantitative measurements of the major reactants and products and a simultaneous direct search for any minor products.…”

mentioning

confidence: 99%

Effects of external ions on the energetics of proton transfers across hydrogen bonds

Scheiner¹,

Redfern²,

Szczȩśniak³

1985

J. Phys. Chem.

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Ions of both positive and negative charge are placed in various locations around H bonds and energetics of proton transfer within the bonds calculated by ab initio molecular orbital methods. Ions examined include Li+, Na+, Cl', (NH4)+, HCOO", and point charges of both signs. These ions are found capable of producing profound effects upon the transfers, with the most marked changes occurring when the ions are positioned along the H-bond axis. Approach of each ion toward the symmetric (H20-H-0H2)+ system introduces progressively greater degrees of asymmetry into the transfer potential. As a cation approaches the nitrogen atom of (H3N-H-OH2)+, a second well appears in this potential which, in the absence of external charges, contains only one minimum. The new well becomes progressively stabilized under closer approach of the ion until the (H3N--HOH2)+ configuration is equal in energy to (H3NH--OH2)+ at a distance of 3 Á. The effects of all ions, including the point charges, are quite similar to one another, particularly for distances greater than 3 Á. The perturbations in the transfer potentials may be modeled quite closely by including the Coulombic interaction between a point charge and the proton undergoing the motion; however, the remaining atoms of the H-bonded system act to magnify to nearly double this effective field.

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mentioning

confidence: 99%

Effects of external ions on the energetics of proton transfers across hydrogen bonds

Scheiner¹,

Redfern²,

Szczȩśniak³

1985

J. Phys. Chem.

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“…Electrostatic interactions can lead to large enhancements in the chemical reaction rates in enzymes compared to their rates in solution; see, e.g., [26]. Comparison of the similarity of electrostatic properties in the vicinity of the catalytic sites of related enzymes can point to important electrostatic properties for the catalytic reaction, as was shown for the catalytic triad of serine proteases [27]. For diffusion-controlled enzymes, electrostatic interactions are important, not only for catalyzing the chemical reaction but also for steering substrates to the active site.…”

Section: Identification Of Electrostatic Features Important For Bindimentioning

confidence: 95%

Protein interaction property similarity analysis

Wade

Gabdoulline

Rienzo

2001

Int J of Quantum Chemistry

105

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ABSTRACT:We describe how similarity indices may be applied to semiquantitatively compare the molecular interaction fields, such as electrostatic and hydrophobic potentials, of proteins. We then review ways in which this approach has been used to investigate protein interaction properties in diverse applications ranging from in-depth comparison of pairs of proteins to large-scale analysis of hundreds of modeled protein structures.

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“…If such a mode of export occurs in archaea, the failure to identify SecA homologs in these organisms may be due to the fact that either (i) the protein(s) involved, although performing a function analogous to SecA, are unrelated to SecA in structure and/or mechanism; or (ii) that an archaeal SecA‐like protein with similar structure and function exists, but lacks any significant amino acid sequence conservation. Several such examples of structural and functional convergent evolution exist among the serine proteases [172–174], as well as in a number of viral coat proteins from eukaryotic viruses and bacteriophage [175–177].…”

Section: Sec‐mediated Protein Translocationmentioning

confidence: 99%

Translocation of proteins across archaeal cytoplasmic membranes

et al. 2004

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All cells need to transport proteins across hydrophobic membranes. Several mechanisms have evolved to facilitate this transport, including: (i) the universally-conserved Sec system, which transports proteins in an unfolded conformation and is thought to be the major translocation pathway in most organisms and (ii) the Tat system, which transports proteins that have already obtained some degree of tertiary structure. Here, we present the current understanding of these processes in the domain Archaea, and how they compare to the corresponding pathways in bacteria and eukaryotes.

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Comparison of protein electrostatic potential along the catalytic triad of serine proteinases

Cited by 40 publications

References 18 publications

Effects of external ions on the energetics of proton transfers across hydrogen bonds

Effects of external ions on the energetics of proton transfers across hydrogen bonds

Protein interaction property similarity analysis

Translocation of proteins across archaeal cytoplasmic membranes

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