Crystallographically observed folded topology of an unsubstituted γ-aminobutyric acid incorporated in a model peptide: importance of a C--H···O interaction.
IR@IMTECH: CSIR-Institute of Microbial Technology, Chandigarh
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| Title |
Crystallographically observed folded topology of an unsubstituted γ-aminobutyric acid incorporated in a model peptide: importance of a C--H···O interaction.
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| Creator |
Kumar, Nigam
Venugopalan, P Kishore, Raghuvansh |
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| Subject |
QD Chemistry
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| Description |
To validate the existing hypothesis put forward by Navarro et al., we performed single crystal X-ray diffraction structural analysis of a designed model peptide incorporating an unsubstituted achiral γ-aminobutyric acid: Boc-Pro-γ-Abu-OH (1) lacking C-terminal amide group. The analysis established existence of an overall unusual tightly folded topology stabilized by a conventional N(i)···H--N(i + 1) and an unconventional C(i)--H···O(i) type intramolecular hydrogen bonding interactions, encompassing a five-membered and a six-membered ring motifs, respectively. Moreover, in conjunction with Fourier transform infrared (FT-IR) absorption study in solid KBr, the results provided evidence that two conventional and one unconventional noncovalent intermolecular interaction stabilize a right-handed helical architecture generated via molecular self-assembly by translating the symmetry related molecules along the crystallographic b axis. © 2010 Wiley Periodicals, Inc. Biopolymers 93: 927-931, 2010.
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| Publisher |
Wiley
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| Date |
2010-11
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Article
PeerReviewed |
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| Format |
application/pdf
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| Identifier |
http://crdd.osdd.net/open/513/1/kishore10.pdf
Kumar, Nigam and Venugopalan, P and Kishore, Raghuvansh (2010) Crystallographically observed folded topology of an unsubstituted γ-aminobutyric acid incorporated in a model peptide: importance of a C--H···O interaction. Biopolymers, 93 (11). pp. 927-31. ISSN 0006-3525 |
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| Relation |
http://onlinelibrary.wiley.com/doi/10.1002/bip.21511/pdf
http://crdd.osdd.net/open/513/ |
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