9 results on '"Scheiner, S."'
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2. A structural role for tryptophan in proteins, and the ubiquitous Trp C δ1 -H...O=C (backbone) hydrogen bond.
- Author
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Szczygiel M, Derewenda U, Scheiner S, Minor W, and Derewenda ZS
- Subjects
- Models, Molecular, Crystallography, X-Ray methods, Protein Conformation, Tryptophan chemistry, Hydrogen Bonding, Proteins chemistry
- Abstract
Tryptophan is the most prominent amino acid found in proteins, with multiple functional roles. Its side chain is made up of the hydrophobic indole moiety, with two groups that act as donors in hydrogen bonds: the N
ϵ -H group, which is a potent donor in canonical hydrogen bonds, and a polarized Cδ1 -H group, which is capable of forming weaker, noncanonical hydrogen bonds. Due to adjacent electron-withdrawing moieties, C-H...O hydrogen bonds are ubiquitous in macromolecules, albeit contingent on the polarization of the donor C-H group. Consequently, Cα -H groups (adjacent to the carbonyl and amino groups of flanking peptide bonds), as well as the Cϵ1 -H and Cδ2 -H groups of histidines (adjacent to imidazole N atoms), are known to serve as donors in hydrogen bonds, for example stabilizing parallel and antiparallel β-sheets. However, the nature and the functional role of interactions involving the Cδ1 -H group of the indole ring of tryptophan are not well characterized. Here, data mining of high-resolution (r ≤ 1.5 Å) crystal structures from the Protein Data Bank was performed and ubiquitous close contacts between the Cδ1 -H groups of tryptophan and a range of electronegative acceptors were identified, specifically main-chain carbonyl O atoms immediately upstream and downstream in the polypeptide chain. The stereochemical analysis shows that most of the interactions bear all of the hallmarks of proper hydrogen bonds. At the same time, their cohesive nature is confirmed by quantum-chemical calculations, which reveal interaction energies of 1.5-3.0 kcal mol-1 , depending on the specific stereochemistry., (open access.)- Published
- 2024
- Full Text
- View/download PDF
3. Theoretical Studies of IR and NMR Spectral Changes Induced by Sigma-Hole Hydrogen, Halogen, Chalcogen, Pnicogen, and Tetrel Bonds in a Model Protein Environment.
- Author
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Michalczyk M, Zierkiewicz W, Wysokiński R, and Scheiner S
- Subjects
- Acetamides chemistry, Hydrogen chemistry, Hydrogen Bonding, Lewis Acids chemistry, Nuclear Magnetic Resonance, Biomolecular, Spectrophotometry, Infrared, Chalcogens chemistry, Halogens chemistry, Proteins chemistry
- Abstract
Various types of σ-hole bond complexes were formed with FX, HFY, H
2 FZ, and H3 FT (X = Cl, Br, I; Y = S, Se, Te; Z = P, As, Sb; T = Si, Ge, Sn) as Lewis acid. In order to examine their interactions with a protein, N-methylacetamide (NMA), a model of the peptide linkage was used as the base. These noncovalent bonds were compared by computational means with H-bonds formed by NMA with XH molecules (X = F, Cl, Br, I). In all cases, the A-F bond, which lies opposite the base and is responsible for the σ-hole on the A atom (A refers to the bridging atom), elongates and its stretching frequency undergoes a shift to the red with a band intensification, much as what occurs for the X-H bond in a H-bond (HB). Unlike the NMR shielding decrease seen in the bridging proton of a H-bond, the shielding of the bridging A atom is increased. The spectroscopic changes within NMA are similar for H-bonds and the other noncovalent bonds. The C=O bond of the amide is lengthened and its stretching frequency red-shifted and intensified. The amide II band shifts to higher frequency and undergoes a small band weakening. The NMR shielding of the O atom directly involved in the bond rises, whereas the C and N atoms both undergo a shielding decrease. The frequency shifts of the amide I and II bands of the base as well as the shielding changes of the three pertinent NMA atoms correlate well with the strength of the noncovalent bond.- Published
- 2019
- Full Text
- View/download PDF
4. Weak H-bonds. Comparisons of CH···O to NH···O in proteins and PH···N to direct P···N interactions.
- Author
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Scheiner S
- Subjects
- Carbon chemistry, Hydrogen Bonding, Nitrogen chemistry, Oxygen chemistry, Phosphorus chemistry, Protein Structure, Secondary, Proteins chemistry
- Abstract
Whereas CH···O H-bonds are usually weaker than interpeptide NH···O H-bonds, this is not necessarily the case within proteins. The nominally weaker CH···O are surprisingly strong, comparable to, and in some cases stronger than, the NH···O H-bonds in the context of the forces that hold together the adjacent strands in protein β-sheets. The peptide NH is greatly weakened as proton donor in certain conformations of the protein backbone, particularly extended structures, and forms correspondingly weaker H-bonds. The PH group is a weak proton donor, but will form PH···N H-bonds. However, there is a stronger interaction in which P can engage, in which the P atom, not the H, directly approaches the N electron donor to establish a direct P···N interaction. This approach is stabilized by the same sort of electron transfer from the N lone pair to the P-H σ* antibond that characterizes the PH···N H-bond.
- Published
- 2011
- Full Text
- View/download PDF
5. Identification of spectroscopic patterns of CH...O H-bonds in proteins.
- Author
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Scheiner S
- Subjects
- Dipeptides chemistry, Hydrogen Bonding, Magnetic Resonance Spectroscopy, Models, Molecular, Protein Conformation, Protons, Proteins chemistry
- Abstract
Ab initio calculations are used to identify characteristics of vibrational and NMR spectra that signal the involvement of a protein backbone in a CH...O H-bond and that distinguish this sort of interaction from other H-bonds in which a protein might participate. Glycine and alanine dipeptides, in both their C7 and C5 minimum-energy structures, are paired with formamide in a number of different H-bonding arrangements. The CH...O H-bond is characterized by a small contraction of the C-H bond length, along with a blue shift in its stretching frequency, accompanied by an intensification of this vibrational band. In the context of NMR spectra, the bridging CH proton's chemical shift is moved downfield by 1-2 ppm. The aforementioned features are not produced by other H-bonds in which the protein backbone might participate, such as NH proton donation or accepting a proton via the peptide C=O.
- Published
- 2009
- Full Text
- View/download PDF
6. Minimum energy pathways for proton transfer between adjacent sites exposed to water.
- Author
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Friedman R, Fischer S, Nachliel E, Scheiner S, and Gutman M
- Subjects
- Algorithms, Binding Sites, Computer Simulation, Fluorescent Dyes chemistry, Models, Chemical, Models, Molecular, Quantum Theory, Surface Properties, Temperature, Fluorescein chemistry, Proteins chemistry, Protons, Water chemistry
- Abstract
The capacity to transfer protons between surface groups is an innate property of many proteins. The transfer of a proton between donor and acceptor, located as far as 6-7 A apart, necessitates the participation of water molecules in the process. In a previous study we investigated the mechanism of proton transfer (PT) between bulk exposed sites, a few ångströms apart, using as a model the proton exchange between the proton-binding sites of the fluorescein molecule in dilute aqueous solution.1 The present study expands the understanding of PT reactions between adjacent sites exposed to water through the calculation the minimum energy pathways (MEPs) by the conjugate peak refinement algorithm2 and a quantum-mechanical potential. The PT reaction trajectories were calculated for the fluorescein system with an increasing number of water molecules. The MEP calculations reveal that the transition state is highly strained and involves a supramolecular structure in which fluorescein and the interconnecting water molecules are covalently bonded together and the protons are shared between neighboring oxygens. These findings are in accord with the high activation energy, as measured for the reaction, and indicate that PT reactions on the surface proceed by a semi- or fully concerted rather than stepwise mechanism. A similar mechanism is assumed to be operative on the surface of proteins and renders water-mediated PT reactions as highly efficient as they are.
- Published
- 2007
- Full Text
- View/download PDF
7. Contributions of NH...O and CH...O hydrogen bonds to the stability of beta-sheets in proteins.
- Author
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Scheiner S
- Subjects
- Databases, Protein, Dimerization, Glycine chemistry, Models, Molecular, Molecular Conformation, Molecular Structure, Peptides chemistry, Protein Conformation, Protein Folding, Protein Structure, Secondary, Thermodynamics, Biophysics methods, Chemistry, Physical methods, Hydrogen Bonding, Proteins chemistry
- Abstract
Ab initio quantum calculations are applied to both the parallel and the antiparallel arrangements of the beta-sheets of proteins. The energies of the NH...O and CH...O hydrogen bonds present in the beta-sheet are evaluated separately from one another by appropriate modifications of the model systems. The bond energies of these two sorts of hydrogen bonds are found to be very nearly equal in the parallel beta-sheet. The NH...O bonds are stronger than CH...O in the antiparallel geometry but only by a relatively small margin. Moreover, the former NH...O bonds are weakened when placed next to one another, as occurs in the antiparallel beta-sheet. As a result, there is little energetic distinction between the NH...O and CH...O bonds in the full antiparallel beta-sheet, just as in the parallel structure.
- Published
- 2006
- Full Text
- View/download PDF
8. Effect of solvent upon CH...O hydrogen bonds with implications for protein folding.
- Author
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Scheiner S and Kar T
- Subjects
- Chemistry, Physical methods, Circular Dichroism, Dimerization, Magnetic Resonance Spectroscopy, Molecular Conformation, Protein Conformation, Protein Folding, Protons, Thermodynamics, Water chemistry, Hydrogen Bonding, Proteins chemistry, Solvents chemistry
- Abstract
The series of CH...O bonds formed between CF(n)H(4-n) (n = 0-3) and water are studied by quantum calculations under vacuum and in various solvents, including aqueous environment. The results are compared with the OH...O bond of the water dimer in the same solvents. Increasing polarity of the solvent leads in all cases to a lessening of the H-bond interaction energy, in a uniform fashion such that the CH...O bonds all remain weaker than OH...O in any solvent. These H-bond weakenings are coupled to a shortening of the inter-subunit separation. The contraction of the covalent CH bond to the bridging proton is reduced as the solvent becomes more polar, and the blue shift of its stretching vibration is likewise diminished. A process is considered that simulates protein folding by starting from a pair of noninteracting subunits in aqueous solvent and then goes to a H-bonded pair within the confines of a protein environment. This process is found to be energetically more favorable for some of the CH...O H-bonds than for the nominally stronger conventional OH...O H-bond. This finding suggests that CH...O bonds can make important energetic contributions to protein folding, on par with those made by traditional H-bonds.
- Published
- 2005
- Full Text
- View/download PDF
9. Modification of pK values caused by change in H-bond geometry.
- Author
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Scheiner S and Hillenbrand EA
- Subjects
- Amines, Electrochemistry, Hydrogen Bonding, Hydrogen-Ion Concentration, Models, Chemical, Protons, Schiff Bases, Proteins
- Abstract
The competition between various groups for a proton is studied by ab initio molecular orbital methods. It is found that reorientations of the two groups involved in a H-bond can reverse the equilibrium position of the proton shared between them. Specifically, the carbonyl and hydroxyl groups were modeled by H2CO and HOH. In the H-bond between these two groups, association of the proton with the carbonyl (H2COH...OH2)+ is favored over the hydroxyl (H2CO...HOH2)+ when the latter group is situated along a lone pair of the carbonyl oxygen. However, displacement of the water to the C = O axis between the two carbonyl lone pairs reverses the situation and (H2CO...HOH2)+ is more stable. A similar reversal of stability is observed in the H-bond involving a Schiff base (modeled by CH2NH) and amine (NH3). In one arrangement where the lone pairs of the two groups point toward one another, the proton prefers the Schiff base to the amine--i.e., (H2CHNH...NH3)+ is more stable than (H2CHN...HNH3)+. On the other hand, rotation of the lone pair of the amine away from the Schiff base nitrogen results in proton transfer across to the amine. These shifts in stability correspond to reversal of relative pK of the groups involved. A fundamental principle emerging from the calculations is that ion-dipole electrostatic interactions favor transfer of a proton to the group that is positioned as closely as possible to the negative end of the dipole moment vector of the other. The ideas developed here suggest a number of means by which conformational changes may be utilized to shift protons from residue to residue within a protein molecule such as an enzyme or bacteriorhodopsin.
- Published
- 1985
- Full Text
- View/download PDF
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