%0 Generic
%A Rai, Rajkishor
%A Aravinda, Subrayashastry
%A Kanagarajadurai, Karuppiah
%A Raghothama, Srinivasarao
%A Shamala, Narayanaswamy
%A Balaram, Padmanabhan
%D 2006
%T Diproline Templates as Folding Nuclei in Designed Peptides.
Conformational Analysis of Synthetic Peptide Helices
Containing Amino Terminal Pro-Pro Segments
%U https://acs.figshare.com/articles/dataset/Diproline_Templates_as_Folding_Nuclei_in_Designed_Peptides_Conformational_Analysis_of_Synthetic_Peptide_Helices_Containing_Amino_Terminal_Pro_Pro_Segments/3075091
%R 10.1021/ja060674v.s001
%2 https://acs.figshare.com/ndownloader/files/4780876
%K trans conformers
%K 25 examples
%K ci
%K PII
%K NMR studies
%K trans form
%K protein crystal structures
%K conformation
%K nucleating helical
%K NOE
%K systems support
%K 462 diproline segments
%K NMR results
%K equilibrium shifts
%K peptide 2. Analysis
%K Similar results
%K NMR time scale
%K energy minimization studies
%K segment residues 2
%K Diproline Templates
%K polyproline II
%K Conformational Analysis
%K DMSO
%X The effect of N-terminal diproline segments in nucleating helical folding in designed peptides
has been studied in two model sequences Piv-Pro-Pro-Aib-Leu-Aib-Phe-OMe (1) and Boc-Aib-Pro-Pro-Aib-Val-Ala-Phe-OMe (2). The structure of 1 in crystals, determined by X-ray diffraction, reveals a helical
(αR) conformation for the segment residues 2 to 5, stabilized by one 4→1 hydrogen bond and two 5→1
interactions. The N-terminus residue, Pro(1) adopts a polyproline II (PII) conformation. NMR studies in
three different solvent systems support a conformation similar to that observed in crystals. In the apolar
solvent CDCl3, NOE data favor the population of both completely helical and partially unfolded structures.
In the former, the Pro-Pro segment adopts an αR-αR conformation, whereas in the latter, a PII-αR structure
is established. The conformational equilibrium shifts in favor of the PII-αR structure in solvents like methanol
and DMSO. A significant population of the Pro(1)-Pro(2) cis conformer is also observed. The NMR results
are consistent with the population of at least three conformational states about Pro-Pro segment: trans
αR-αR, trans PII-αR and cis PII-αR. Of these, the two trans conformers are in rapid dynamic exchange on the
NMR time scale, whereas the interconversion between cis and trans form is slow. Similar results are obtained
with peptide 2. Analysis of 462 diproline segments in protein crystal structures reveals 25 examples of the
αR-αR conformation followed by a helix. Modeling and energy minimization studies suggest that both PII-αR
and αR-αR conformations have very similar energies in the model hexapeptide 1.
%I ACS Publications