期刊
BIOPOLYMERS
卷 71, 期 5, 页码 558-568出版社
JOHN WILEY & SONS INC
DOI: 10.1002/bip.10534
关键词
tripeptides; random-coil state; proteins; polyproline; proline-containing tripeptides; amide 1 '
资金
- NATIONAL CENTER FOR RESEARCH RESOURCES [P20RR016439] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [S06GM008102] Funding Source: NIH RePORTER
- NCRR NIH HHS [P20 RR16439-01] Funding Source: Medline
- NIGMS NIH HHS [S06GM008102-3052] Funding Source: Medline
Tripeptides serve 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 3(1)-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 psi and phi values in the range of 175degrees-165degrees and -70degrees-(-80degrees), respectively. This is fully confirmed by the respective electronic ultraviolet-CDspectra. 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. (C) 2003 Wiley Periodicals, Inc.
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