PMID- 19562756
OWN - NLM
STAT- MEDLINE
DCOM- 20091006
LR  - 20090805
IS  - 0006-3525 (Print)
IS  - 0006-3525 (Linking)
VI  - 91
IP  - 10
DP  - 2009 Oct
TI  - Natural abundant solid state NMR studies in designed tripeptides for 
      differentiation of multiple conformers.
PG  - 851-60
LID - 10.1002/bip.21270 [doi]
AB  - Solid state NMR (SSNMR) experiments on heteronuclei in natural abundance are 
      described for three synthetically designed tripeptides 
      Piv-(L)Pro-(L)Pro-(L)Phe-OMe (1), Piv-(D)Pro-(L)Pro-(L)Phe-OMe (2), and 
      Piv-(D)Pro-(L)Pro-(L)Phe-NHMe (3). These peptides exist in different conformation 
      as shown by solution state NMR and single crystal X-ray analysis (Chatterjee et 
      al., Chem Eur J 2008, 14, 6192). In this study, SSNMR has been used to probe the 
      conformations of these peptides in their powder form. The (13)C spectrum of 
      peptide (1) showed doubling of resonances corresponding to cis/cis form, unlike 
      in solution where the similar doubling is attributed to cis/trans form. This has 
      been confirmed by the chemical shift differences of C(beta) and C(gamma) carbon 
      of Proline in peptide (1) both in solution and SSNMR. Peptide (2) and (3) 
      provided single set of resonances which represented all trans form across the 
      di-Proline segment. The results are in agreement with the X-ray analysis. Solid 
      state (15)N resonances, especially from Proline residues provided additional 
      information, which is normally not observable in solution state NMR. (1)H 
      chemical shifts are also obtained from a two-dimensional heteronuclear 
      correlation experiment between (1)H--(13)C. The results confirm the utility of 
      NMR as a useful tool for identifying different conformers in peptides in the 
      solid state.
CI  - (c) 2009 Wiley Periodicals, Inc. Biopolymers 91: 851-860, 2009.
FAU - Jayanthi, S
AU  - Jayanthi S
AD  - Department of Physics, Indian Institute of Science, Bangalore 560 012, India.
FAU - Chatterjee, Bhaswati
AU  - Chatterjee B
FAU - Raghothama, S
AU  - Raghothama S
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Biopolymers
JT  - Biopolymers
JID - 0372525
RN  - 0 (Peptides)
SB  - IM
MH  - Magnetic Resonance Spectroscopy
MH  - Molecular Conformation
MH  - Peptides/*chemistry
EDAT- 2009/06/30 09:00
MHDA- 2009/10/07 06:00
CRDT- 2009/06/30 09:00
PHST- 2009/06/30 09:00 [entrez]
PHST- 2009/06/30 09:00 [pubmed]
PHST- 2009/10/07 06:00 [medline]
AID - 10.1002/bip.21270 [doi]
PST - ppublish
SO  - Biopolymers. 2009 Oct;91(10):851-60. doi: 10.1002/bip.21270.