Action of Molybdenum Dioxide Upon Silver Salts.

Smith, Edgar F.; Shinn, Owen L.

doi:10.1021/ja02106a012

Cited by 7 publications

(4 citation statements)

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“…Whereas conventional hydrogen bonds that involve electronegative atoms like oxygen and nitrogen have been thoroughly studied over the decades since their first introduction into the literature and are presently well understood (1)(2)(3), the same cannot be said for the CH⅐⅐O interaction, which is only now gaining wide acceptance as a genuine hydrogen bond (H-bond) 1 (4,5). Although normally weaker than its conventional OH⅐⅐O cousin, the CH⅐⅐O interaction is thought to be crucial in a large number of molecular complexes and crystal structures (6 -10).…”

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

278

237

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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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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

278

237

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“…[4] The importance of conventional interactions such as hydrogen bonds (mentioned above as strong hydrogen bonds), salt bridges and hydrophobicity in protein oligomers are well established. [5,6] A set of weaker interactions have also been recognized to play an important role in the stability and structure of proteins. [7,8] The existence of non-canonical interactions was well documented very early but their importance was not timely appreciated.…”

Section: Introductionmentioning

confidence: 99%

“…Accordingly, hydrogen bonds like OH⋅⋅⋅O, NH⋅⋅⋅O, OH⋅⋅⋅N and NH⋅⋅⋅N may be considered to be strong, whereas interactions like CH⋅⋅⋅O, CH⋅⋅⋅N, OH⋅⋅⋅π, NH⋅⋅⋅π and CH⋅⋅⋅π are weak 4. The importance of conventional interactions such as hydrogen bonds (mentioned above as strong hydrogen bonds), salt bridges and hydrophobicity in protein oligomers are well established 5,6…”

Section: Introductionmentioning

confidence: 99%

Contribution of Non‐Canonical Interactions to the Stability of Sm/LSm Oligomeric Assemblies

Stojanović

Isenović

Zarić

2011

Molecular Informatics

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The distinguishing property of Sm/LSm protein assemblies is their high stability. In order to better understand the nature of Sm/LSm protein oligomers in this study we have analyzed the contribution of non-canonical interactions to the stability of assemblies. The predominant types of non-canonical interactions at Sm/LSm protein interfaces are CH⋅⋅⋅O, and CH⋅⋅⋅N interactions represented at interfaces. Our results show low percentages of XH-π and non-canonical interactions involving sulfur atoms, while the backbone groups were less frequently involved. The data show a high percentage of non-canonical interactions in interfaces formed by charged residues with Lys and Arg, these being the major charged donors. The main chain non-canonical interactions might be slightly more linear than the side chain interactions, and they have somewhat shorter median distances. Comparing the stabilizing amino acid residues with amino acids which build non-canonical interactions at interfaces shows that certain amino acids like Phe, Pro, His and Tyr are involved with a high percentage. The high conservation score of amino acids that are involved in non-canonical interactions in protein interfaces is an additional strong argument for their importance in the stabilization of Sm/LSm protein assemblies.

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“…The classical H-bonds that involve electronegative atoms like oxygen and nitrogen have been thoroughly studied over the decades since their first introduction into literature and are presently well understood [1][2][3]. CH· · ·O interactions are now accepted as a genuine hydrogen bond [4,5].…”

Section: Introductionmentioning

confidence: 99%