| pubmed-article:7811930 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7811930 | lifeskim:mentions | umls-concept:C0004654 | lld:lifeskim |
| pubmed-article:7811930 | lifeskim:mentions | umls-concept:C0205329 | lld:lifeskim |
| pubmed-article:7811930 | lifeskim:mentions | umls-concept:C0205396 | lld:lifeskim |
| pubmed-article:7811930 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
| pubmed-article:7811930 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:7811930 | pubmed:dateCreated | 1995-2-8 | lld:pubmed |
| pubmed-article:7811930 | pubmed:abstractText | Glucose-embedded bacteriorhodopsin shows M-intermediates with different Amide I infrared bands when samples are illuminated at 240 or 260 K, in contrast with fully hydrated samples where a single M-intermediate is formed at all temperatures. In hydrated, but not in glucose-embedded specimens, the N intermediate is formed together with M at 260 K. Both Fourier transform infrared and electron diffraction data from glucose-embedded bacteriorhodopsin suggest that at 260 K a mixture is formed of the M-state that is trapped at 240 K, and a different M-intermediate (MN) that is also formed by mutant forms of bacteriorhodopsin that lack a carboxyl group at the 96 position, necessary for the M to N transition. The fact that an MN species is trapped in glucose-embedded, wild-type bacteriorhodopsin suggests that the glucose samples lack functionally important water molecules that are needed for the proton transfer aspartate 96 to the Schiff base (and, thus, to form the N-intermediate); thus, aspartate 96 is rendered ineffective as a proton donor. | lld:pubmed |
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| pubmed-article:7811930 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7811930 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7811930 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7811930 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7811930 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:7811930 | pubmed:issn | 0006-3495 | lld:pubmed |
| pubmed-article:7811930 | pubmed:author | pubmed-author:GlaeserR MRM | lld:pubmed |
| pubmed-article:7811930 | pubmed:author | pubmed-author:BurkartVV | lld:pubmed |
| pubmed-article:7811930 | pubmed:author | pubmed-author:PerkinsG AGA | lld:pubmed |
| pubmed-article:7811930 | pubmed:author | pubmed-author:VonckJJ | lld:pubmed |
| pubmed-article:7811930 | pubmed:author | pubmed-author:HanB GBG | lld:pubmed |
| pubmed-article:7811930 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7811930 | pubmed:volume | 67 | lld:pubmed |
| pubmed-article:7811930 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7811930 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7811930 | pubmed:pagination | 1173-8 | lld:pubmed |
| pubmed-article:7811930 | pubmed:dateRevised | 2010-9-10 | lld:pubmed |
| pubmed-article:7811930 | pubmed:meshHeading | pubmed-meshheading:7811930-... | lld:pubmed |
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| pubmed-article:7811930 | pubmed:meshHeading | pubmed-meshheading:7811930-... | lld:pubmed |
| pubmed-article:7811930 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:7811930 | pubmed:articleTitle | Two progressive substrates of the M-intermediate can be identified in glucose-embedded, wild-type bacteriorhodopsin. | lld:pubmed |
| pubmed-article:7811930 | pubmed:affiliation | Life Sciences Division, Donner Laboratory, Lawrence Berkeley Laboratory, Berkeley, California 94720. | lld:pubmed |
| pubmed-article:7811930 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7811930 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7811930 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:7811930 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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