Comparison of the Solution Conformation and Dynamics of Antifreeze Glycoproteins from Antarctic Fish
ABSTRACT The 1 H- and 13 C-NMR spectra of antifreeze glycoprotein fractions 1–5 from Antarctic cod have been assigned, and the dynamics have been measured using 13 C relaxation at two temperatures. The chemical shifts and absence of non-sequential 1 H- 1 H NOEs are inconsistent with a folded, compac...
Main Authors: | , , , , , |
---|---|
Other Authors: | |
Format: | Text |
Language: | English |
Published: |
2000
|
Subjects: | |
Online Access: | http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.132.9135 http://www.biophysj.org/cgi/reprint/78/6/3195.pdf |
id |
ftciteseerx:oai:CiteSeerX.psu:10.1.1.132.9135 |
---|---|
record_format |
openpolar |
spelling |
ftciteseerx:oai:CiteSeerX.psu:10.1.1.132.9135 2023-05-15T13:43:38+02:00 Comparison of the Solution Conformation and Dynamics of Antifreeze Glycoproteins from Antarctic Fish Andrew N. Lane Lisa M. Hays Nelly Tsvetkova Robert E. Feeney Lois M. Crowe John H. Crowe The Pennsylvania State University CiteSeerX Archives 2000 application/pdf http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.132.9135 http://www.biophysj.org/cgi/reprint/78/6/3195.pdf en eng http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.132.9135 http://www.biophysj.org/cgi/reprint/78/6/3195.pdf Metadata may be used without restrictions as long as the oai identifier remains attached to it. http://www.biophysj.org/cgi/reprint/78/6/3195.pdf text 2000 ftciteseerx 2016-01-07T14:36:31Z ABSTRACT The 1 H- and 13 C-NMR spectra of antifreeze glycoprotein fractions 1–5 from Antarctic cod have been assigned, and the dynamics have been measured using 13 C relaxation at two temperatures. The chemical shifts and absence of non-sequential 1 H- 1 H NOEs are inconsistent with a folded, compact structure. 13 C relaxation measurements show that the protein has no significant long-range order, and that the local correlation times are adequately described by a random coil model. Hydroxyl protons of the sugar residues were observed at low temperature, and the presence of exchange-mediated ROEs to the sugar indicate extensive hydration. The conformational properties of AFGP1–5 are compared with those of the previously examined 14-mer analog AFGP8, which contains proline residues in place of some alanine residues (Lane, A. N., L. M. Hays, R. E. Feeney, L. M. Crowe, and J. H. Crowe. 1998. Protein Sci. 7:1555–1563). The infrared (IR) spectra of AFGP8 and AFGP1–5 in the amide I region are quite different. The presence of a wide distribution of backbone torsion angles in AFGP1–5 leads to a rich spectrum of frequencies in the IR spectrum, as interconversion among conformational states is slow on the IR frequency time scale. However, these transitions are fast on the NMR chemical shift time scales. The restricted motions for AFGP8 may imply a narrower distribution of possible ø, � angles, as is observed in the IR spectrum. This has significance for attempts to quantify secondary structures of proteins by IR in the presence of extensive loops. Text Antarc* Antarctic Unknown Antarctic |
institution |
Open Polar |
collection |
Unknown |
op_collection_id |
ftciteseerx |
language |
English |
description |
ABSTRACT The 1 H- and 13 C-NMR spectra of antifreeze glycoprotein fractions 1–5 from Antarctic cod have been assigned, and the dynamics have been measured using 13 C relaxation at two temperatures. The chemical shifts and absence of non-sequential 1 H- 1 H NOEs are inconsistent with a folded, compact structure. 13 C relaxation measurements show that the protein has no significant long-range order, and that the local correlation times are adequately described by a random coil model. Hydroxyl protons of the sugar residues were observed at low temperature, and the presence of exchange-mediated ROEs to the sugar indicate extensive hydration. The conformational properties of AFGP1–5 are compared with those of the previously examined 14-mer analog AFGP8, which contains proline residues in place of some alanine residues (Lane, A. N., L. M. Hays, R. E. Feeney, L. M. Crowe, and J. H. Crowe. 1998. Protein Sci. 7:1555–1563). The infrared (IR) spectra of AFGP8 and AFGP1–5 in the amide I region are quite different. The presence of a wide distribution of backbone torsion angles in AFGP1–5 leads to a rich spectrum of frequencies in the IR spectrum, as interconversion among conformational states is slow on the IR frequency time scale. However, these transitions are fast on the NMR chemical shift time scales. The restricted motions for AFGP8 may imply a narrower distribution of possible ø, � angles, as is observed in the IR spectrum. This has significance for attempts to quantify secondary structures of proteins by IR in the presence of extensive loops. |
author2 |
The Pennsylvania State University CiteSeerX Archives |
format |
Text |
author |
Andrew N. Lane Lisa M. Hays Nelly Tsvetkova Robert E. Feeney Lois M. Crowe John H. Crowe |
spellingShingle |
Andrew N. Lane Lisa M. Hays Nelly Tsvetkova Robert E. Feeney Lois M. Crowe John H. Crowe Comparison of the Solution Conformation and Dynamics of Antifreeze Glycoproteins from Antarctic Fish |
author_facet |
Andrew N. Lane Lisa M. Hays Nelly Tsvetkova Robert E. Feeney Lois M. Crowe John H. Crowe |
author_sort |
Andrew N. Lane |
title |
Comparison of the Solution Conformation and Dynamics of Antifreeze Glycoproteins from Antarctic Fish |
title_short |
Comparison of the Solution Conformation and Dynamics of Antifreeze Glycoproteins from Antarctic Fish |
title_full |
Comparison of the Solution Conformation and Dynamics of Antifreeze Glycoproteins from Antarctic Fish |
title_fullStr |
Comparison of the Solution Conformation and Dynamics of Antifreeze Glycoproteins from Antarctic Fish |
title_full_unstemmed |
Comparison of the Solution Conformation and Dynamics of Antifreeze Glycoproteins from Antarctic Fish |
title_sort |
comparison of the solution conformation and dynamics of antifreeze glycoproteins from antarctic fish |
publishDate |
2000 |
url |
http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.132.9135 http://www.biophysj.org/cgi/reprint/78/6/3195.pdf |
geographic |
Antarctic |
geographic_facet |
Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
http://www.biophysj.org/cgi/reprint/78/6/3195.pdf |
op_relation |
http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.132.9135 http://www.biophysj.org/cgi/reprint/78/6/3195.pdf |
op_rights |
Metadata may be used without restrictions as long as the oai identifier remains attached to it. |
_version_ |
1766191375934554112 |