2014
DOI: 10.1021/ja503107h
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Evidence of an Unusual N–H···N Hydrogen Bond in Proteins

Abstract: Many residues within proteins adopt conformations that appear to be stabilized by interactions between an amide N–H and the amide N of the previous residue. To explore whether these interactions constitute hydrogen bonds, we characterized the IR stretching frequencies of deuterated variants of proline and the corresponding carbamate, as well as the four proline residues of an Src homology 3 domain protein. The CδD2 stretching frequencies are shifted to lower energies due to hyperconjugation with N i electron … Show more

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Cited by 48 publications
(73 citation statements)
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“…The crystal structure exhibited an endo proline ring pucker, a cis Boc-proline bond, and main chain torsion angles ϕ , ψ that were ideal for β-turn formation ( ϕ , ψ = −77°, +1°, near the ideal values for the i +2 residue of type I (−90°, 0°), type II′ (−80°, 0°), or type VIa1 (−90°, 0°) β-turns). 12 This conformation was also observed in the crystal structure of Ac-hyp-OMe (CSD: EMITEA; ϕ , ψ = −84°, +18°). 13 β-turns are central components of protein structure, 12a, b, 14 and are also common recognition motifs in protein-protein interactions, 15 suggesting the use of this amino acid (and other 4 S -substituted prolines) in the stabilization of β-turn motifs in peptides and proteins and in molecular recognition.…”
Section: Resultssupporting
confidence: 57%
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“…The crystal structure exhibited an endo proline ring pucker, a cis Boc-proline bond, and main chain torsion angles ϕ , ψ that were ideal for β-turn formation ( ϕ , ψ = −77°, +1°, near the ideal values for the i +2 residue of type I (−90°, 0°), type II′ (−80°, 0°), or type VIa1 (−90°, 0°) β-turns). 12 This conformation was also observed in the crystal structure of Ac-hyp-OMe (CSD: EMITEA; ϕ , ψ = −84°, +18°). 13 β-turns are central components of protein structure, 12a, b, 14 and are also common recognition motifs in protein-protein interactions, 15 suggesting the use of this amino acid (and other 4 S -substituted prolines) in the stabilization of β-turn motifs in peptides and proteins and in molecular recognition.…”
Section: Resultssupporting
confidence: 57%
“…12 This conformation was also observed in the crystal structure of Ac-hyp-OMe (CSD: EMITEA; ϕ , ψ = −84°, +18°). 13 β-turns are central components of protein structure, 12a, b, 14 and are also common recognition motifs in protein-protein interactions, 15 suggesting the use of this amino acid (and other 4 S -substituted prolines) in the stabilization of β-turn motifs in peptides and proteins and in molecular recognition. 16 …”
Section: Resultssupporting
confidence: 57%
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“…This behavior is the reverse of the Bohlmann effect, 5457 where a “negative” hyperconjugation transfers electron density from a lone pair orbital to an optimally positioned C–H σ * orbital. This decreases the C–H bond order and substantially downshifts the C–H stretching frequencies.…”
Section: Resultsmentioning
confidence: 96%