An investigation by dielectric methods of hydration in myoglobin solutions
The permittivities of three solutions of sperm-whale myoglobin of different concentrations were measured in the frequency range 300–1300MHz at 20°C by using a coaxial-line technique. These results were combined with those measured previously at frequencies below 10MHz. Two methods are described for...
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ftpubmed:oai:pubmedcentral.nih.gov:1166293 2023-05-15T18:26:41+02:00 An investigation by dielectric methods of hydration in myoglobin solutions Grant, Edward H. Mitton, Barbara G. R. South, Gerald P. Sheppard, Rodney J. 1974-05 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1166293 http://www.ncbi.nlm.nih.gov/pubmed/4475592 en eng http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1166293 http://www.ncbi.nlm.nih.gov/pubmed/4475592 Proteins Text 1974 ftpubmed 2013-08-30T11:22:36Z The permittivities of three solutions of sperm-whale myoglobin of different concentrations were measured in the frequency range 300–1300MHz at 20°C by using a coaxial-line technique. These results were combined with those measured previously at frequencies below 10MHz. Two methods are described for calculating the extent of macromolecular hydration from the data. The more reliable method yields results of approx. 0.25g of H2O/g of protein, which is in satisfactory agreement with the theoretically calculated value. Agreement with the value found from the rotational motion of the molecule is not so close, which is probably caused by the different meanings that may be ascribed to the term hydration. Text Sperm whale PubMed Central (PMC) |
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PubMed Central (PMC) |
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English |
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Proteins |
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Proteins Grant, Edward H. Mitton, Barbara G. R. South, Gerald P. Sheppard, Rodney J. An investigation by dielectric methods of hydration in myoglobin solutions |
topic_facet |
Proteins |
description |
The permittivities of three solutions of sperm-whale myoglobin of different concentrations were measured in the frequency range 300–1300MHz at 20°C by using a coaxial-line technique. These results were combined with those measured previously at frequencies below 10MHz. Two methods are described for calculating the extent of macromolecular hydration from the data. The more reliable method yields results of approx. 0.25g of H2O/g of protein, which is in satisfactory agreement with the theoretically calculated value. Agreement with the value found from the rotational motion of the molecule is not so close, which is probably caused by the different meanings that may be ascribed to the term hydration. |
format |
Text |
author |
Grant, Edward H. Mitton, Barbara G. R. South, Gerald P. Sheppard, Rodney J. |
author_facet |
Grant, Edward H. Mitton, Barbara G. R. South, Gerald P. Sheppard, Rodney J. |
author_sort |
Grant, Edward H. |
title |
An investigation by dielectric methods of hydration in myoglobin solutions |
title_short |
An investigation by dielectric methods of hydration in myoglobin solutions |
title_full |
An investigation by dielectric methods of hydration in myoglobin solutions |
title_fullStr |
An investigation by dielectric methods of hydration in myoglobin solutions |
title_full_unstemmed |
An investigation by dielectric methods of hydration in myoglobin solutions |
title_sort |
investigation by dielectric methods of hydration in myoglobin solutions |
publishDate |
1974 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1166293 http://www.ncbi.nlm.nih.gov/pubmed/4475592 |
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Sperm whale |
genre_facet |
Sperm whale |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1166293 http://www.ncbi.nlm.nih.gov/pubmed/4475592 |
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1766208662111518720 |