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The Crystal-Solution Problem of Sperm Whale Myoglobin

The central question to be discussed in this paper is whether the structure established for sperm whale myoglobin in the crystalline state is the same as that of the protein in solution. As judged by its ultraviolet optical rotatory dispersion, the helical content of metmyoglobin in solution does no...

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Autor principal: Urnes, Peter
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1965
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2195474/
https://www.ncbi.nlm.nih.gov/pubmed/5859928
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author Urnes, Peter
author_facet Urnes, Peter
author_sort Urnes, Peter
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description The central question to be discussed in this paper is whether the structure established for sperm whale myoglobin in the crystalline state is the same as that of the protein in solution. As judged by its ultraviolet optical rotatory dispersion, the helical content of metmyoglobin in solution does not differ from that in the crystal, 77 per cent. Although an uncertainty of about ±5 per cent must attach to this result, it excludes many alternative arrangements of the polypeptide chain. The folding of the chain may be further restricted to the basic form seen in the crystal if the dimensions of the molecule in solution and the interactions of specific chemical groups are taken into account. Since the rotatory dispersion of metmyoglobin is constant with respect to ionic strength, and since the dispersions of reduced and oxymyoglobin reveal no change in helical content upon their formation from metmyoglobin, one may infer that the structure of the protein is largely maintained both as it dissolves and during its reversible combination with oxygen. The crystallographic model of myoglobin thus offers a structural basis for attempting to explain its physiological function in solution. The relevance of this conclusion to the crystal-solution problems presented by other species of protein is then best seen in the light of common factors that govern the equilibrium of all proteins between crystal and solution.
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spelling pubmed-21954742008-04-23 The Crystal-Solution Problem of Sperm Whale Myoglobin Urnes, Peter J Gen Physiol Oxygen-Transporting Pigments The central question to be discussed in this paper is whether the structure established for sperm whale myoglobin in the crystalline state is the same as that of the protein in solution. As judged by its ultraviolet optical rotatory dispersion, the helical content of metmyoglobin in solution does not differ from that in the crystal, 77 per cent. Although an uncertainty of about ±5 per cent must attach to this result, it excludes many alternative arrangements of the polypeptide chain. The folding of the chain may be further restricted to the basic form seen in the crystal if the dimensions of the molecule in solution and the interactions of specific chemical groups are taken into account. Since the rotatory dispersion of metmyoglobin is constant with respect to ionic strength, and since the dispersions of reduced and oxymyoglobin reveal no change in helical content upon their formation from metmyoglobin, one may infer that the structure of the protein is largely maintained both as it dissolves and during its reversible combination with oxygen. The crystallographic model of myoglobin thus offers a structural basis for attempting to explain its physiological function in solution. The relevance of this conclusion to the crystal-solution problems presented by other species of protein is then best seen in the light of common factors that govern the equilibrium of all proteins between crystal and solution. The Rockefeller University Press 1965-09-01 /pmc/articles/PMC2195474/ /pubmed/5859928 Text en Copyright © 1965 by The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Oxygen-Transporting Pigments
Urnes, Peter
The Crystal-Solution Problem of Sperm Whale Myoglobin
title The Crystal-Solution Problem of Sperm Whale Myoglobin
title_full The Crystal-Solution Problem of Sperm Whale Myoglobin
title_fullStr The Crystal-Solution Problem of Sperm Whale Myoglobin
title_full_unstemmed The Crystal-Solution Problem of Sperm Whale Myoglobin
title_short The Crystal-Solution Problem of Sperm Whale Myoglobin
title_sort crystal-solution problem of sperm whale myoglobin
topic Oxygen-Transporting Pigments
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2195474/
https://www.ncbi.nlm.nih.gov/pubmed/5859928
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