Direct observation of hydrogen atom dynamics and interactions by ultrahigh resolution neutron protein crystallography

Chen, Julian C.-H.; Hanson, B. Leif; Fisher, S.Z.; Langan, Paul; Kovalevsky, Andrey

doi:10.1073/pnas.1208341109

Cited by 57 publications

(38 citation statements)

References 43 publications

(52 reference statements)

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“…Finally, a very recently determined ultra-high-resolution neutron structure of the protein crambin emphasizes that CH⅐⅐⅐O hydrogen bonds represent only one class of a large category of underappreciated interactions in biomolecules (69). In addition to many CH⅐⅐⅐O hydrogen bonds, the authors directly observed many acceptor hydrogen bonds.…”

Section: Discussionmentioning

confidence: 91%

Carbon-Oxygen Hydrogen Bonding in Biological Structure and Function

Horowitz

Trievel

2012

Journal of Biological Chemistry

286

249

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Carbon-oxygen (CH⅐⅐⅐O) hydrogen bonding represents an unusual category of molecular interactions first documented in biological structures over 4 decades ago. Although CH⅐⅐⅐O hydrogen bonding has remained generally underappreciated in the biochemical literature, studies over the last 15 years have begun to yield direct evidence of these interactions in biological systems. In this minireview, we provide a historical context of biological CH⅐⅐⅐O hydrogen bonding and summarize some major advancements from experimental studies over the past several years that have elucidated the importance, prevalence, and functions of these interactions. In particular, we examine the impact of CH⅐⅐⅐O bonds on protein and nucleic acid structure, molecular recognition, and enzyme catalysis and conclude by exploring overarching themes and unresolved questions regarding unconventional interactions in biomolecular structure.

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Section: Discussionmentioning

confidence: 91%

Carbon-Oxygen Hydrogen Bonding in Biological Structure and Function

Horowitz

Trievel

2012

Journal of Biological Chemistry

286

249

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“…46 Evidence for more (acidic) labile C-H groups has also come from H/D exchange patterns in the atomic resolution neutron structures of cobalamin and crambin. 14,15 The case of crambin is particularly interesting because it involves partial exchange of one of the H atoms bound to a C α (on Gly31), evidence of potential C-H. . .O H-bonding.…”

Section: Unusual Chemical Bonds Involving Hydrogenmentioning

confidence: 99%

Seeing the chemistry in biology with neutron crystallography

Langan

Chen

2013

Phys. Chem. Chem. Phys.

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New developments in macromolecular neutron crystallography have led to an increasing number of structures published over the last decade. Hydrogen atoms, normally invisible in most X-ray crystal structures, become visible in neutron structures. Using X-rays allows one to see structure, while neutrons allow one to reveal the chemistry inherent in these macromolecular structures. A number of surprising and sometimes controversial results have emerged from recent neutron structures; because it is difficult to see or predict hydrogen atoms in X-ray structures, when they are seen by neutrons they can be in unexpected locations with important chemical and biological consequences. Here we describe examples of chemistry seen with neutrons for the first time in biological macromolecules over the past few years.

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“…They have been proposed [209] to act as the principal driving force for folding of β,γ-hybrid model peptide and of the structure of amicyanin [210]. Ultrahigh resolution neutron diffraction data of proteins [211] have noted CH··O HBs with an average HB length of 2.0 Å. These bonds are essential ingredients of oligosaccharides and carbohydrates where they have been estimated [198] to account for as much as 40 % of the total interaction energy.…”

Section: Other Systemsmentioning

confidence: 97%

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

Scheiner

2015

Challenges and Advances in Computational Chemistry and Physics

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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.

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Direct observation of hydrogen atom dynamics and interactions by ultrahigh resolution neutron protein crystallography

Cited by 57 publications

References 43 publications

Carbon-Oxygen Hydrogen Bonding in Biological Structure and Function

Carbon-Oxygen Hydrogen Bonding in Biological Structure and Function

Seeing the chemistry in biology with neutron crystallography

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

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