Contribution of CH· · ·X Hydrogen Bonds to Biomolecular Structure

Scheiner, Steve

doi:10.1007/978-1-4020-4853-1_7

Cited by 27 publications

(26 citation statements)

References 151 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…31,32 A later review 33 extended the summary to work up through 2005, with a particular emphasis on the sources of the unexpected blue shift of the C-H stretching frequency [34][35][36][37][38][39][40][41] that occurs on occasion. The potential for such weak H-bonds to contribute to biomolecular structure was the focus of some later reviews, 42,43 as well as consideration of the effect of immersion of these systems in solvent, 44,45 and cooperativity effects. 16,[46][47][48][49] Section 2 below focuses on one particular aspect of the manner and degree to which CHÁ Á ÁO H-bonds might affect the structure of biomolecules.…”

Section: Steve Scheinermentioning

confidence: 99%

Weak H-bonds. Comparisons of CH⋯O to NH⋯O in proteins and PH⋯N to direct P⋯N interactions

Scheiner

2011

Phys. Chem. Chem. Phys.

Self Cite

171

View full text Add to dashboard Cite

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.

show abstract

Section: Steve Scheinermentioning

confidence: 99%

Weak H-bonds. Comparisons of CH⋯O to NH⋯O in proteins and PH⋯N to direct P⋯N interactions

Scheiner

2011

Phys. Chem. Chem. Phys.

Self Cite

171

View full text Add to dashboard Cite

show abstract

“…Some of our earlier work up through 2006 has been summarized already [71][72][73] so will only be briefly outlined here, with emphasis on major findings. Beginning with the simplest system which might contain a CH··O HB, the binding energy between CH 4 and OH 2 , is very weak [74], on the order of 0.5 kcal/mol or less.…”

Section: Recent Workmentioning

confidence: 99%

The CH‥O H-Bond as a Determining Factor in Molecular Structure

Scheiner

2015

Challenges and Advances in Computational Chemistry and Physics

Self Cite

View full text Add to dashboard Cite

The factors that affect the strength of CH··O hydrogen bonds (HBs) are enumerated, along with the source of their stability, and the structural and spectroscopic features that signal their presence. Their influence upon a number of chemical and biological processes is discussed. Within the context of proteins, the C α H group of protein residues can engage in CH··O HBs, as can the CH groups of a number of amino acid side chains including aromatic residues. CH··O HBs have the potential to make a major contribution to protein folding, particularly in an aqueous environment. These unconventional HBs may play as important a role in the formation of protein β-sheet structures as do NH··O HBs. The strength of CH··O HBs is magnified several-fold by the presence of positive charge on the proton donor. The implications of these principles are discussed for a number of specific biological and chemical problems, which include the catalytic mechanisms of methyltransferases and serine proteases, and the structural properties of fluoroamides.

show abstract

“…Pyrimidine molecules are constrained to reduced molecular motion within the ice due to C−H•••N weak hydrogen bonds among them. 47 On the top surface, pyrimidine molecules are expected to be antiparallel aligned in respect to their dipole moments in a planar configuration reminiscent from that found in the isolated dimer. 43 In this scenario, the protonated parent cation may be formed according to the scheme presented in Figure 6.…”

Section: +2mentioning

confidence: 99%

Fragmentation and Ion Desorption from Condensed Pyrimidine by Electron Impact: Implications for Cometary and Interstellar Heterocyclic Chemistry

Ribeiro¹,

Almeida²,

Wolff³

et al. 2014

J. Phys. Chem. C

View full text Add to dashboard Cite

The desorption process induced by photons, electrons, or ions onto icy surfaces is an important mechanism for leading neutral or ionized molecular species to the gas phase in interstellar and circumstellar environments. In this work, we report the results of high energy electron impact onto a condensed pyrimidine ice by means of electron-stimulated ion desorption (ESID). Desorbed cations from the icy surface were analyzed by time-of-flight mass spectrometry (TOF-MS). The most abundant desorbed ions are H + and H 2 + , although several other fragments, such as C

show abstract

Contribution of CH· · ·X Hydrogen Bonds to Biomolecular Structure

Cited by 27 publications

References 151 publications

Weak H-bonds. Comparisons of CH⋯O to NH⋯O in proteins and PH⋯N to direct P⋯N interactions

Weak H-bonds. Comparisons of CH⋯O to NH⋯O in proteins and PH⋯N to direct P⋯N interactions

The CH‥O H-Bond as a Determining Factor in Molecular Structure

Fragmentation and Ion Desorption from Condensed Pyrimidine by Electron Impact: Implications for Cometary and Interstellar Heterocyclic Chemistry

Contact Info

Product

Resources

About