Natural abundance carbon 13 nuclear magnetic resonance spectroscopy of antifreeze glycoproteins.

E. Berman; A. Allerhand; A. L. DeVries

Natural abundance carbon 13 nuclear magnetic resonance spectroscopy of antifreeze glycoproteins.

E. Berman, A. Allerhand, A. L. DeVries

Research output: Contribution to journal › Article › peer-review

Abstract

Natural abundance 13C NMR spectroscopy (at 67.9 MHz) is used to study an aqueous solution of the antifreeze glycoproteins 3 to 6 from the Antarctic cod. Assignments of resonances to specific carbons of the known Ala-Ala-[beta Gal-(1 leads to 3)-alpha-N-acetylgalactosamine]Thr repeating unit are presented. Some of the carbons of the proline residues of glycoprotein 6 are also identified. Spin-lattice relaxation times (at 30 degrees C), linewidths (at 35 degrees C), nuclear Overhauser enhancements (at 35 degrees C), and the temperature dependence of chemical shifts (from 0 degrees to 75 degrees C) all strongly suggest that these antifreeze glycoproteins are predominantly or entirely flexible random coil polymers.

Original language	English (US)
Pages (from-to)	4407-4410
Number of pages	4
Journal	Journal of Biological Chemistry
Volume	255
Issue number	10
State	Published - May 25 1980
Externally published	Yes

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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title = "Natural abundance carbon 13 nuclear magnetic resonance spectroscopy of antifreeze glycoproteins.",

abstract = "Natural abundance 13C NMR spectroscopy (at 67.9 MHz) is used to study an aqueous solution of the antifreeze glycoproteins 3 to 6 from the Antarctic cod. Assignments of resonances to specific carbons of the known Ala-Ala-[beta Gal-(1 leads to 3)-alpha-N-acetylgalactosamine]Thr repeating unit are presented. Some of the carbons of the proline residues of glycoprotein 6 are also identified. Spin-lattice relaxation times (at 30 degrees C), linewidths (at 35 degrees C), nuclear Overhauser enhancements (at 35 degrees C), and the temperature dependence of chemical shifts (from 0 degrees to 75 degrees C) all strongly suggest that these antifreeze glycoproteins are predominantly or entirely flexible random coil polymers.",

author = "E. Berman and A. Allerhand and DeVries, {A. L.}",

note = "Copyright: Medline is the source for the citation and abstract of this record.",

year = "1980",

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language = "English (US)",

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T1 - Natural abundance carbon 13 nuclear magnetic resonance spectroscopy of antifreeze glycoproteins.

AU - Berman, E.

AU - Allerhand, A.

AU - DeVries, A. L.

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PY - 1980/5/25

Y1 - 1980/5/25

N2 - Natural abundance 13C NMR spectroscopy (at 67.9 MHz) is used to study an aqueous solution of the antifreeze glycoproteins 3 to 6 from the Antarctic cod. Assignments of resonances to specific carbons of the known Ala-Ala-[beta Gal-(1 leads to 3)-alpha-N-acetylgalactosamine]Thr repeating unit are presented. Some of the carbons of the proline residues of glycoprotein 6 are also identified. Spin-lattice relaxation times (at 30 degrees C), linewidths (at 35 degrees C), nuclear Overhauser enhancements (at 35 degrees C), and the temperature dependence of chemical shifts (from 0 degrees to 75 degrees C) all strongly suggest that these antifreeze glycoproteins are predominantly or entirely flexible random coil polymers.

AB - Natural abundance 13C NMR spectroscopy (at 67.9 MHz) is used to study an aqueous solution of the antifreeze glycoproteins 3 to 6 from the Antarctic cod. Assignments of resonances to specific carbons of the known Ala-Ala-[beta Gal-(1 leads to 3)-alpha-N-acetylgalactosamine]Thr repeating unit are presented. Some of the carbons of the proline residues of glycoprotein 6 are also identified. Spin-lattice relaxation times (at 30 degrees C), linewidths (at 35 degrees C), nuclear Overhauser enhancements (at 35 degrees C), and the temperature dependence of chemical shifts (from 0 degrees to 75 degrees C) all strongly suggest that these antifreeze glycoproteins are predominantly or entirely flexible random coil polymers.

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