Conformational properties of native sperm whale apomyoglobin in solution
Abstract Apomyoglobin from sperm whale is often used for studies of ligand binding, protein folding, and protein stability. In an effort to describe its conformational properties in solution, homonuclear and heteronuclear ( 13 C and 15 N) NMR methods were applied to the protein in its native state....
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crwiley:10.1110/ps.8.7.1484 2024-06-02T08:14:52+00:00 Conformational properties of native sperm whale apomyoglobin in solution Lecomte, JULIETTE T.J. Sukits, Steven F. Bhattacharya, Shibani Falzone, Christopher J. 1999 http://dx.doi.org/10.1110/ps.8.7.1484 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1110%2Fps.8.7.1484 https://onlinelibrary.wiley.com/doi/pdf/10.1110/ps.8.7.1484 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor Protein Science volume 8, issue 7, page 1484-1491 ISSN 0961-8368 1469-896X journal-article 1999 crwiley https://doi.org/10.1110/ps.8.7.1484 2024-05-03T10:51:54Z Abstract Apomyoglobin from sperm whale is often used for studies of ligand binding, protein folding, and protein stability. In an effort to describe its conformational properties in solution, homonuclear and heteronuclear ( 13 C and 15 N) NMR methods were applied to the protein in its native state. Assignments were confirmed for nuclear Overhauser effects (NOEs) involving side chain and backbone protons in the folded regions of the structure. These NOEs were used to derive distance restraints. The shifts induced by the hydrophobic dye 8‐anilino‐1‐naphthalenesulfonic acid (ANS) were inspected in the regions remote from its binding site and served as an indicator of conformational flexibility. 3 J αH‐NH values were obtained to assess dihedral angle averaging and to provide additional restraints. A family of structures was calculated with X‐PLOR and an ab initio simulated annealing protocol using holomyoglobin as a template. Where the structure appeared well defined by chemical shift, line width, ANS perturbation, and density of NOEs, the low resolution model of apomyoglobin provides a valid approximation for the structure. The new model offers an improved representation of the folded regions of the protein, which encompass the A, B, E, helices as well as parts of the G and H helices. Regions that are less well defined at this stage of calculations include the CD corner and the end of the H‐helix. The EF‐F‐FG segment remains uncharacterized. Article in Journal/Newspaper Sperm whale Wiley Online Library Protein Science 8 7 1484 1491 |
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English |
description |
Abstract Apomyoglobin from sperm whale is often used for studies of ligand binding, protein folding, and protein stability. In an effort to describe its conformational properties in solution, homonuclear and heteronuclear ( 13 C and 15 N) NMR methods were applied to the protein in its native state. Assignments were confirmed for nuclear Overhauser effects (NOEs) involving side chain and backbone protons in the folded regions of the structure. These NOEs were used to derive distance restraints. The shifts induced by the hydrophobic dye 8‐anilino‐1‐naphthalenesulfonic acid (ANS) were inspected in the regions remote from its binding site and served as an indicator of conformational flexibility. 3 J αH‐NH values were obtained to assess dihedral angle averaging and to provide additional restraints. A family of structures was calculated with X‐PLOR and an ab initio simulated annealing protocol using holomyoglobin as a template. Where the structure appeared well defined by chemical shift, line width, ANS perturbation, and density of NOEs, the low resolution model of apomyoglobin provides a valid approximation for the structure. The new model offers an improved representation of the folded regions of the protein, which encompass the A, B, E, helices as well as parts of the G and H helices. Regions that are less well defined at this stage of calculations include the CD corner and the end of the H‐helix. The EF‐F‐FG segment remains uncharacterized. |
format |
Article in Journal/Newspaper |
author |
Lecomte, JULIETTE T.J. Sukits, Steven F. Bhattacharya, Shibani Falzone, Christopher J. |
spellingShingle |
Lecomte, JULIETTE T.J. Sukits, Steven F. Bhattacharya, Shibani Falzone, Christopher J. Conformational properties of native sperm whale apomyoglobin in solution |
author_facet |
Lecomte, JULIETTE T.J. Sukits, Steven F. Bhattacharya, Shibani Falzone, Christopher J. |
author_sort |
Lecomte, JULIETTE T.J. |
title |
Conformational properties of native sperm whale apomyoglobin in solution |
title_short |
Conformational properties of native sperm whale apomyoglobin in solution |
title_full |
Conformational properties of native sperm whale apomyoglobin in solution |
title_fullStr |
Conformational properties of native sperm whale apomyoglobin in solution |
title_full_unstemmed |
Conformational properties of native sperm whale apomyoglobin in solution |
title_sort |
conformational properties of native sperm whale apomyoglobin in solution |
publisher |
Wiley |
publishDate |
1999 |
url |
http://dx.doi.org/10.1110/ps.8.7.1484 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1110%2Fps.8.7.1484 https://onlinelibrary.wiley.com/doi/pdf/10.1110/ps.8.7.1484 |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_source |
Protein Science volume 8, issue 7, page 1484-1491 ISSN 0961-8368 1469-896X |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1110/ps.8.7.1484 |
container_title |
Protein Science |
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8 |
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7 |
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1484 |
op_container_end_page |
1491 |
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1800738873666437120 |