Name
Abstract | ||
|---|---|---|
The full conformational space was explored for an achiral and two chiral beta-peptide models: namely For-beta-Ala-NH(2). For-beta-Abu-NH(2), and For-beta-Aib-NH(2). Stability and conformational properties of all three model systems were computed at different levels of theory: RHF/3-21G, B3LYP/6-311 + + G(d,p)//RHF/3-21G, B3LYP/6-311 + + G(d,p), MP2//B3LYP/6-311 + + G(d,p), CCSD//B3LYP/6-311 + + G(d,p), and CCSD(T)//B3LYP/6-311 + + G(d,p). In addition, ab initio, E = E(phi, mu, psi) potential energy hypersurfaces of all three models were determined, and their topologies were analyzed to determine the inherent flexibility properties of these beta-peptide models. Fewer points were found and assigned than expected on the basis of Multidimensional Conformational Analysis (MDCA). Furthermore, it has been demonstrated, that the four-dimensional surface, E = E(phi, mu, psi), can be reduced into a three-dimensional one: E = E[phi, f(phi), psi]. This reduction of dimensionality of freedom of motion suggests that beta-peptides are less flexible than one would have thought. This agrees with experimental data published on the conformational properties of peptides composed of beta-amino acid residues. |
Year | DOI | Venue |
|---|---|---|
2004 | 10.1002/jcc.10357 | JOURNAL OF COMPUTATIONAL CHEMISTRY |
Keywords | Field | DocType |
beta-peptides,ab initio and DFT computation,structure and stability,Ramachandran surface,flexibility,conformation and topology,beta-amino acids | Mathematical optimization,Biochemical engineering,Chemistry | Journal |
Volume | Issue | ISSN |
25 | 2 | 0192-8651 |
Citations | PageRank | References |
0 | 0.34 | 1 |
Authors | ||
3 | ||
Name | Order | Citations | PageRank |
|---|---|---|---|
| Tamás Beke | 1 | 0 | 1.01 |
| Imre G. Csizmadia | 2 | 24 | 10.22 |
| András Perczel | 3 | 39 | 16.63 |