Cyclic peptides fulfil a diversity of biologically important functions by acting as hormones, toxins, antiobiotics, ion carriers, inhibitors etc. and in vivo activity is intimately related to their molecular conformations.
Minimum energy conformations of proline-containing helices
β Scribed by Alexander Polinsky; Murray Goodman; Karen A. Williams; Charles M. Deber
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1992
- Tongue
- English
- Weight
- 555 KB
- Volume
- 32
- Category
- Article
- ISSN
- 0006-3525
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
A global optimization method is described for identifying the global minimum energy conformation, as well as lower and upper bounds on the global minimum conformer of solvated peptides. In considering the effects of hydration, two independent continuum-based solvation models are employed. The first
In order to evaluate the influenceof cyclic secondaryamino acids on the stability of ~-turn structure,we have preparedAc-Gly-L-Xxx-L-Leu-Gly -N(CH3)2(Xxx= Aze, 4-memberedring: 1, Xxx = Pro, 5-memberedring: 2, Xxx = Pip, 6-memberedring: 3). The NOE cross peaks that support $turn structure were observ
As proline plays an important role in biologically active peptides, many analogues of this residue have been developed to modulate the proportion of cis and trans conformers. A correlation between the pyrrolidine ring shape and structural properties of proline has been established. Diketopiperazine
## Abstract The role of Nβterminus diproline segments in facilitating helical folding in short peptides has been investigated in a set of model hexapeptides of the type Pivβ**XxxβYyy**βAibβLeuβAibβPheβOMe (Piv, pivaloyl). Nine sequences have been investigated with the following Nβterminus dipeptide