The role played by C–H...O and C–H...N interactions in determining molecular packing and conformation

Berkovitch‐Yellin, Z.; Leiserowitz, Leslie

doi:10.1107/s0108768184001919

Cited by 227 publications

(84 citation statements)

References 13 publications

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“…The formation of this 3D structure may rest simply on optimal packing. Alternatively it is rationalized by cooperative C-H···O interactions 7 (total length 3.39 Å) between each amide oxygen and a pyridyl C-H belonging to an adjacent bilayer.…”

Section: Take Down Policymentioning

confidence: 99%

Hydrogen-bonded porous solid derived from trimesic amide

Palmans

Vekemans

Kooijman³

et al. 1997

Chem. Commun.

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Section: Take Down Policymentioning

confidence: 99%

Hydrogen-bonded porous solid derived from trimesic amide

Palmans

Vekemans

Kooijman³

et al. 1997

Chem. Commun.

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“…It was noted some time ago that the crystal structures of various amino acids contain these interactions (28), but their importance to larger protein segments such as ␣-glycine (29) has been revealed as well. Other groups that appear to be involved in CH⅐⅐O H-bonding include the aryl groups of aromatic residues like phenylalanine (30), the C ␦ H of proline (31), the CH groups of histidine (32,33), and the lysine C ⑀ H and valine C ␥2 H groups (34).…”

Section: From the Department Of Chemistry And Biochemistry Utah Statmentioning

confidence: 99%

Strength of the CαH··O Hydrogen Bond of Amino Acid Residues

Scheiner

Kar

2001

Journal of Biological Chemistry

286

239

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Although the peptide C␣ H group has historically not been thought to form hydrogen bonds within proteins, ab initio quantum calculations show it to be a potent proton donor. Its binding energy to a water molecule lies in the range between 1.9 and 2.5 kcal/mol for nonpolar and polar amino acids; the hydrogen bond (H-bond) involving the charged lysine residue is even stronger than a conventional OH⅐⅐O interaction. The preferred H-bond lengths are quite uniform, about 3.32 Å. Formation of each interaction results in a downfield shift of the bridging hydrogen's chemical shift and a blue shift in the C ␣ H stretching frequency, potential diagnostics of the presence of such an H-bond within a protein.

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“…The orthorhombic unit cell contains four discrete molecules (Fig. 1) of the title compound; each asymmetric unit contains one complete molecule with no atom sitting at a special position, separated by normal van der Waals distances (Bondi, 1964) and some weak hydrogen bonds (Berkovitch-Yellin & Leiserowitz, 1984) ( Table 2). A view of the puckering of the title compound, including the adopted numbering scheme, is presented in Fig.…”

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confidence: 99%