Cross-polarization 13C nuclear magnetic resonance spectroscopy of collagen

Jacob Schaefer, E. O. Stejskal, Curtis F. Brewer, Harold D. Keiser, H. Sternlicht

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

Natural abundance 13C nuclear magnetic resonance (nmr) spectra have been obtained for samples of a variety of native collagens by use of cross-polarization (CP) techniques which permit high resolution natural abundance 13C nmr spectra of solids to be obtained with high sensitivity. The CP 13C nmr spectra of lyophilized skin and tendon collagens consisted of two broad resonance envelopes spanning a five kHz range. Hydrated tendon collagen gave rise to a CP spectrum very similar to that obtained for the lyophilized sample, indicating that it retains its solid-like properties. In contrast, hydrated skin collagen became denatured under the conditions of the CP experiment and subsequently gave rise to a conventional high-resolution Fourier transform (FT) nmr spectrum. The CP 13C nmr spectrum of ivory was similar to those of lyophilized skin and tendon collagens, demonstrating the solid-like character of the collagen in dentine, whereas the CP spectrum of bovine nasal cartilage reflected the presence of highly mobile proteoglycan components in addition to relatively rigid collagen molecules. In the case of ivory, the resolution of the CP spectrum was enhanced by "magic angle" spinning to a degree approaching that of conventional FT 13C nmr spectra of denatured collagen in solution. Because of its ability to probe the dynamic properties of solid-like biological molecules, CP 13C nmr spectroscopy should be a valuable investigative tool for future studies.

Original languageEnglish (US)
Pages (from-to)657-661
Number of pages5
JournalArchives of Biochemistry and Biophysics
Volume190
Issue number2
DOIs
StatePublished - 1978

Fingerprint

Nuclear magnetic resonance spectroscopy
Magnetic Resonance Spectroscopy
Collagen
Polarization
Nuclear magnetic resonance
Tendons
Skin
Fourier Analysis
Fourier transforms
Nasal Cartilages
Magic angle spinning
Molecules
Cartilage
Proteoglycans
Dentin
Experiments

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Cross-polarization 13C nuclear magnetic resonance spectroscopy of collagen. / Schaefer, Jacob; Stejskal, E. O.; Brewer, Curtis F.; Keiser, Harold D.; Sternlicht, H.

In: Archives of Biochemistry and Biophysics, Vol. 190, No. 2, 1978, p. 657-661.

Research output: Contribution to journalArticle

Schaefer, Jacob ; Stejskal, E. O. ; Brewer, Curtis F. ; Keiser, Harold D. ; Sternlicht, H. / Cross-polarization 13C nuclear magnetic resonance spectroscopy of collagen. In: Archives of Biochemistry and Biophysics. 1978 ; Vol. 190, No. 2. pp. 657-661.
@article{3726ba5abd554810b56209593b539119,
title = "Cross-polarization 13C nuclear magnetic resonance spectroscopy of collagen",
abstract = "Natural abundance 13C nuclear magnetic resonance (nmr) spectra have been obtained for samples of a variety of native collagens by use of cross-polarization (CP) techniques which permit high resolution natural abundance 13C nmr spectra of solids to be obtained with high sensitivity. The CP 13C nmr spectra of lyophilized skin and tendon collagens consisted of two broad resonance envelopes spanning a five kHz range. Hydrated tendon collagen gave rise to a CP spectrum very similar to that obtained for the lyophilized sample, indicating that it retains its solid-like properties. In contrast, hydrated skin collagen became denatured under the conditions of the CP experiment and subsequently gave rise to a conventional high-resolution Fourier transform (FT) nmr spectrum. The CP 13C nmr spectrum of ivory was similar to those of lyophilized skin and tendon collagens, demonstrating the solid-like character of the collagen in dentine, whereas the CP spectrum of bovine nasal cartilage reflected the presence of highly mobile proteoglycan components in addition to relatively rigid collagen molecules. In the case of ivory, the resolution of the CP spectrum was enhanced by {"}magic angle{"} spinning to a degree approaching that of conventional FT 13C nmr spectra of denatured collagen in solution. Because of its ability to probe the dynamic properties of solid-like biological molecules, CP 13C nmr spectroscopy should be a valuable investigative tool for future studies.",
author = "Jacob Schaefer and Stejskal, {E. O.} and Brewer, {Curtis F.} and Keiser, {Harold D.} and H. Sternlicht",
year = "1978",
doi = "10.1016/0003-9861(78)90323-5",
language = "English (US)",
volume = "190",
pages = "657--661",
journal = "Archives of Biochemistry and Biophysics",
issn = "0003-9861",
publisher = "Academic Press Inc.",
number = "2",

}

TY - JOUR

T1 - Cross-polarization 13C nuclear magnetic resonance spectroscopy of collagen

AU - Schaefer, Jacob

AU - Stejskal, E. O.

AU - Brewer, Curtis F.

AU - Keiser, Harold D.

AU - Sternlicht, H.

PY - 1978

Y1 - 1978

N2 - Natural abundance 13C nuclear magnetic resonance (nmr) spectra have been obtained for samples of a variety of native collagens by use of cross-polarization (CP) techniques which permit high resolution natural abundance 13C nmr spectra of solids to be obtained with high sensitivity. The CP 13C nmr spectra of lyophilized skin and tendon collagens consisted of two broad resonance envelopes spanning a five kHz range. Hydrated tendon collagen gave rise to a CP spectrum very similar to that obtained for the lyophilized sample, indicating that it retains its solid-like properties. In contrast, hydrated skin collagen became denatured under the conditions of the CP experiment and subsequently gave rise to a conventional high-resolution Fourier transform (FT) nmr spectrum. The CP 13C nmr spectrum of ivory was similar to those of lyophilized skin and tendon collagens, demonstrating the solid-like character of the collagen in dentine, whereas the CP spectrum of bovine nasal cartilage reflected the presence of highly mobile proteoglycan components in addition to relatively rigid collagen molecules. In the case of ivory, the resolution of the CP spectrum was enhanced by "magic angle" spinning to a degree approaching that of conventional FT 13C nmr spectra of denatured collagen in solution. Because of its ability to probe the dynamic properties of solid-like biological molecules, CP 13C nmr spectroscopy should be a valuable investigative tool for future studies.

AB - Natural abundance 13C nuclear magnetic resonance (nmr) spectra have been obtained for samples of a variety of native collagens by use of cross-polarization (CP) techniques which permit high resolution natural abundance 13C nmr spectra of solids to be obtained with high sensitivity. The CP 13C nmr spectra of lyophilized skin and tendon collagens consisted of two broad resonance envelopes spanning a five kHz range. Hydrated tendon collagen gave rise to a CP spectrum very similar to that obtained for the lyophilized sample, indicating that it retains its solid-like properties. In contrast, hydrated skin collagen became denatured under the conditions of the CP experiment and subsequently gave rise to a conventional high-resolution Fourier transform (FT) nmr spectrum. The CP 13C nmr spectrum of ivory was similar to those of lyophilized skin and tendon collagens, demonstrating the solid-like character of the collagen in dentine, whereas the CP spectrum of bovine nasal cartilage reflected the presence of highly mobile proteoglycan components in addition to relatively rigid collagen molecules. In the case of ivory, the resolution of the CP spectrum was enhanced by "magic angle" spinning to a degree approaching that of conventional FT 13C nmr spectra of denatured collagen in solution. Because of its ability to probe the dynamic properties of solid-like biological molecules, CP 13C nmr spectroscopy should be a valuable investigative tool for future studies.

UR - http://www.scopus.com/inward/record.url?scp=0018197720&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0018197720&partnerID=8YFLogxK

U2 - 10.1016/0003-9861(78)90323-5

DO - 10.1016/0003-9861(78)90323-5

M3 - Article

C2 - 718170

AN - SCOPUS:0018197720

VL - 190

SP - 657

EP - 661

JO - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

SN - 0003-9861

IS - 2

ER -