A conformation-specific IR spectroscopic signature for weak CO⋯CO n→π* interaction in capped 4R-hydroxyproline
| Autor: | Satish Kumar, Kamal K. Mishra, Shahaji H. More, Aloke Das, Santosh K. Singh, Krishna N. Ganesh |
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| Rok vydání: | 2019 |
| Předmět: |
Chemistry
Hydrogen bond General Physics and Astronomy Infrared spectroscopy Sequence (biology) 02 engineering and technology 010402 general chemistry 021001 nanoscience & nanotechnology 01 natural sciences 0104 chemical sciences chemistry.chemical_compound Hydroxyproline Residue (chemistry) Crystallography Monomer Physical and Theoretical Chemistry 0210 nano-technology Polyproline helix Triple helix |
| Zdroj: | Physical Chemistry Chemical Physics. 21:4755-4762 |
| ISSN: | 1463-9084 1463-9076 |
| Popis: | Collagen, the most abundant protein in animals, has a unique triple helical structure comprising three parallel left-handed polyproline II (PPII) strands while each of the strands consists of a repeating sequence of X–Y–Gly, where X = proline (Pro) and Y = 4-hydroxyproline (Hyp). Collagen forms a stable triple helix of very long polypeptide strands despite the absence of intra-strand hydrogen bonding in the individual polypeptide chains. It has been reported that non-covalent n→π* interaction plays a significant role in stabilizing the individual polypeptide strands in collagen. However, there is no direct spectroscopic evidence for the presence of this interaction in collagen or its building block. Herein, we have observed for the first time a conformation-specific IR spectroscopic signature for CO⋯CO n→π*-amide interaction in a capped Hyp residue, the most important monomer building block of collagen, using isolated gas phase IR spectroscopy and quantum chemistry calculations. The proof of the existence of this interaction in a model monomer has implications for better understanding of its role not only in structures of collagen but also most of the other proteins and larger peptides. |
| Databáze: | OpenAIRE |
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