13 C NMR Relaxation Studies of Molecular Motion in Peptide Fragments from Human Transthyretin

Jacqueline A. Jarvis, David J. Craik

Research output: Contribution to journalArticleResearchpeer-review

12 Citations (Scopus)

Abstract

Natural-abundance 13 C T 1 and NOE measurements have been made for backbone and side-chain sites in peptide fragments of transthyretin (TTR 10-20, TTR 105-115, and TTR 105-115 Met111 ) at 13 C Larmor frequencies of 125 and 75 MHz. These peptides have previously been implicated in the formation of amyloid fibrils, The data were systematically assessed for their consistency with theoretical relaxation parameters derived from models of molecular motion, It was shown that of four models, ranging from simple isotropic motion to one defining internal wobbling of the 13 C- 1 H vector, the "model-free approach" (Lipari and Szabo, J. Am. Chem. Soc.104, 4546, 1982) was best able to predict the experimental data, These peptides exhibited overall correlation times close to 1 ns. Internal motions with effective correlation times of 0.08 ns were observed for backbone carbon sites, and side-chain carbons exhibited more rapid and less ordered motions, No indication of retarded motion due to the presence of small peptide aggregates was detected, in agreement with reports of the rapid incorporation of these species into amyloid fibrils.

Original languageEnglish
Pages (from-to)95-106
Number of pages12
JournalJournal of Magnetic Resonance, Series B
Volume107
Issue number2
DOIs
Publication statusPublished - 7 May 1995

Cite this

@article{f6ec7fb3a0dc4e6e83a3cc4014f3f56b,
title = "13 C NMR Relaxation Studies of Molecular Motion in Peptide Fragments from Human Transthyretin",
abstract = "Natural-abundance 13 C T 1 and NOE measurements have been made for backbone and side-chain sites in peptide fragments of transthyretin (TTR 10-20, TTR 105-115, and TTR 105-115 Met111 ) at 13 C Larmor frequencies of 125 and 75 MHz. These peptides have previously been implicated in the formation of amyloid fibrils, The data were systematically assessed for their consistency with theoretical relaxation parameters derived from models of molecular motion, It was shown that of four models, ranging from simple isotropic motion to one defining internal wobbling of the 13 C- 1 H vector, the {"}model-free approach{"} (Lipari and Szabo, J. Am. Chem. Soc.104, 4546, 1982) was best able to predict the experimental data, These peptides exhibited overall correlation times close to 1 ns. Internal motions with effective correlation times of 0.08 ns were observed for backbone carbon sites, and side-chain carbons exhibited more rapid and less ordered motions, No indication of retarded motion due to the presence of small peptide aggregates was detected, in agreement with reports of the rapid incorporation of these species into amyloid fibrils.",
author = "Jarvis, {Jacqueline A.} and Craik, {David J.}",
year = "1995",
month = "5",
day = "7",
doi = "10.1006/jmrb.1995.1065",
language = "English",
volume = "107",
pages = "95--106",
journal = "Journal of Magnetic Resonance, Series B",
issn = "1064-1866",
number = "2",

}

13 C NMR Relaxation Studies of Molecular Motion in Peptide Fragments from Human Transthyretin. / Jarvis, Jacqueline A.; Craik, David J.

In: Journal of Magnetic Resonance, Series B, Vol. 107, No. 2, 07.05.1995, p. 95-106.

Research output: Contribution to journalArticleResearchpeer-review

TY - JOUR

T1 - 13 C NMR Relaxation Studies of Molecular Motion in Peptide Fragments from Human Transthyretin

AU - Jarvis, Jacqueline A.

AU - Craik, David J.

PY - 1995/5/7

Y1 - 1995/5/7

N2 - Natural-abundance 13 C T 1 and NOE measurements have been made for backbone and side-chain sites in peptide fragments of transthyretin (TTR 10-20, TTR 105-115, and TTR 105-115 Met111 ) at 13 C Larmor frequencies of 125 and 75 MHz. These peptides have previously been implicated in the formation of amyloid fibrils, The data were systematically assessed for their consistency with theoretical relaxation parameters derived from models of molecular motion, It was shown that of four models, ranging from simple isotropic motion to one defining internal wobbling of the 13 C- 1 H vector, the "model-free approach" (Lipari and Szabo, J. Am. Chem. Soc.104, 4546, 1982) was best able to predict the experimental data, These peptides exhibited overall correlation times close to 1 ns. Internal motions with effective correlation times of 0.08 ns were observed for backbone carbon sites, and side-chain carbons exhibited more rapid and less ordered motions, No indication of retarded motion due to the presence of small peptide aggregates was detected, in agreement with reports of the rapid incorporation of these species into amyloid fibrils.

AB - Natural-abundance 13 C T 1 and NOE measurements have been made for backbone and side-chain sites in peptide fragments of transthyretin (TTR 10-20, TTR 105-115, and TTR 105-115 Met111 ) at 13 C Larmor frequencies of 125 and 75 MHz. These peptides have previously been implicated in the formation of amyloid fibrils, The data were systematically assessed for their consistency with theoretical relaxation parameters derived from models of molecular motion, It was shown that of four models, ranging from simple isotropic motion to one defining internal wobbling of the 13 C- 1 H vector, the "model-free approach" (Lipari and Szabo, J. Am. Chem. Soc.104, 4546, 1982) was best able to predict the experimental data, These peptides exhibited overall correlation times close to 1 ns. Internal motions with effective correlation times of 0.08 ns were observed for backbone carbon sites, and side-chain carbons exhibited more rapid and less ordered motions, No indication of retarded motion due to the presence of small peptide aggregates was detected, in agreement with reports of the rapid incorporation of these species into amyloid fibrils.

UR - http://www.scopus.com/inward/record.url?scp=0029299006&partnerID=8YFLogxK

U2 - 10.1006/jmrb.1995.1065

DO - 10.1006/jmrb.1995.1065

M3 - Article

VL - 107

SP - 95

EP - 106

JO - Journal of Magnetic Resonance, Series B

JF - Journal of Magnetic Resonance, Series B

SN - 1064-1866

IS - 2

ER -