Journal article
The structure of tri‐proline in water probed by polarized Raman, Fourier transform infrared, vibrational circular dichroism, and electric ultraviolet circular dichroism spectroscopy
Peptide Science, v 71(5), pp 558-568
2003
PMID: 14635096
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Tripeptidesserve as model systems for understanding the so‐called random‐coil state of peptides and proteins. While it is well known that polyproline or proline‐rich polypeptides adopt the very regular polyproline‐II (PPII) or left‐handed 31‐helix conformation, it was thus far not clear whether this is also the predominant structure adopted by proline‐containing tripeptides. To clarify this issue, we have investigated the amide I′ band profile in the ir, isotropic, and anisotropic Raman, and vibrational circular dichroism (VCD) spectrum of cationic and zwitterionic tri‐proline in D2O. The data were analyzed by modifying a recently developed algorithm, which allows one to obtain the central dihedral angles of tripeptides from the amide I′ band intensities (R. Schweitzer‐Stenner, Biophysical Journal, 2002, Vol. 83, pp. 523–532). Our analysis revealed that the peptide adopts a nearly canonical PPII structure in water with ψ and ϕ values in the range of 175°–165° and −70°–(−80°), respectively. This is fully confirmed by the respective electronic ultraviolet‐CD spectra. Our result indicates that the strong PPII propensity of trans proline results from local interactions between the pyrrolidine ring and the backbone and is not due to any long‐range interactions. © 2003 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 71: 558–568, 2003
Metrics
Details
- Title
- The structure of tri‐proline in water probed by polarized Raman, Fourier transform infrared, vibrational circular dichroism, and electric ultraviolet circular dichroism spectroscopy
- Creators
- Reinhard Schweitzer‐StennerFatma EkerAlejandro PerezKai GriebenowXiaolin CaoLaurence A Nafie
- Publication Details
- Peptide Science, v 71(5), pp 558-568
- Publisher
- Wiley Subscription Services, Inc., A Wiley Company; Hoboken
- Number of pages
- 11
- Grant note
- Fondos Institucionales para la Investigación of the University of Puerto Rico (UPR) (20‐02‐2‐78‐514) NIH‐SCORE (S06 GM008102‐3052) Center for Research in Protein Structure, Function and Dynamics (CRPSFD) (P20 RR16439‐01)
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Chemistry
- Web of Science ID
- WOS:000186962300003
- Scopus ID
- 2-s2.0-0344305773
- Other Identifier
- 991014878309604721
UN Sustainable Development Goals (SDGs)
This publication has contributed to the advancement of the following goals:
InCites Highlights
Data related to this publication, from InCites Benchmarking & Analytics tool:
- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology
- Biophysics