| pubmed-article:9925773 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9925773 | lifeskim:mentions | umls-concept:C0596901 | lld:lifeskim |
| pubmed-article:9925773 | lifeskim:mentions | umls-concept:C0004654 | lld:lifeskim |
| pubmed-article:9925773 | lifeskim:mentions | umls-concept:C1521991 | lld:lifeskim |
| pubmed-article:9925773 | lifeskim:mentions | umls-concept:C0205148 | lld:lifeskim |
| pubmed-article:9925773 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:9925773 | lifeskim:mentions | umls-concept:C0184967 | lld:lifeskim |
| pubmed-article:9925773 | lifeskim:mentions | umls-concept:C0449830 | lld:lifeskim |
| pubmed-article:9925773 | lifeskim:mentions | umls-concept:C0302891 | lld:lifeskim |
| pubmed-article:9925773 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:9925773 | pubmed:dateCreated | 1999-3-25 | lld:pubmed |
| pubmed-article:9925773 | pubmed:abstractText | Bacteriorhodopsin is the one of the best-studied models of an ion pump. Five atomic models are now available, yet their comparison reveals differences of some loops connecting the seven transmembrane alpha-helices. In an attempt to resolve this enigma, topographs were recorded in aqueous solution with the atomic force microscope (AFM) to reveal the most native surface structure of bacteriorhodopsin molecules in the purple membrane. Individual peptide loops were observed with a lateral resolution of between 4.5 A and 5.8 A, and a vertical resolution of about 1 A. The AFM images demonstrate for the first time, that the shape, the position, and the flexibility of individual polypeptide loops depend on the packing arrangement of bacteriorhodopsin molecules in the lipid bilayer. | lld:pubmed |
| pubmed-article:9925773 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9925773 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9925773 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9925773 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9925773 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9925773 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9925773 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:9925773 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:9925773 | pubmed:author | pubmed-author:EngelAA | lld:pubmed |
| pubmed-article:9925773 | pubmed:author | pubmed-author:BüldtGG | lld:pubmed |
| pubmed-article:9925773 | pubmed:author | pubmed-author:MüllerD JDJ | lld:pubmed |
| pubmed-article:9925773 | pubmed:author | pubmed-author:SassH JHJ | lld:pubmed |
| pubmed-article:9925773 | pubmed:author | pubmed-author:MüllerS ASA | lld:pubmed |
| pubmed-article:9925773 | pubmed:copyrightInfo | Copyright 1998 Academic Press. | lld:pubmed |
| pubmed-article:9925773 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9925773 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:9925773 | pubmed:volume | 285 | lld:pubmed |
| pubmed-article:9925773 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9925773 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9925773 | pubmed:pagination | 1903-9 | lld:pubmed |
| pubmed-article:9925773 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:9925773 | pubmed:meshHeading | pubmed-meshheading:9925773-... | lld:pubmed |
| pubmed-article:9925773 | pubmed:meshHeading | pubmed-meshheading:9925773-... | lld:pubmed |
| pubmed-article:9925773 | pubmed:meshHeading | pubmed-meshheading:9925773-... | lld:pubmed |
| pubmed-article:9925773 | pubmed:meshHeading | pubmed-meshheading:9925773-... | lld:pubmed |
| pubmed-article:9925773 | pubmed:meshHeading | pubmed-meshheading:9925773-... | lld:pubmed |
| pubmed-article:9925773 | pubmed:meshHeading | pubmed-meshheading:9925773-... | lld:pubmed |
| pubmed-article:9925773 | pubmed:meshHeading | pubmed-meshheading:9925773-... | lld:pubmed |
| pubmed-article:9925773 | pubmed:meshHeading | pubmed-meshheading:9925773-... | lld:pubmed |
| pubmed-article:9925773 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:9925773 | pubmed:articleTitle | Surface structures of native bacteriorhodopsin depend on the molecular packing arrangement in the membrane. | lld:pubmed |
| pubmed-article:9925773 | pubmed:affiliation | M. E. Müller-Institute for Microscopic Structural Biology, Biozentrum University of Basel, Klingelbergstrasse 70, Basel, CH-4056, Switzerland. muellerda@ubaclu.unibas.ch | lld:pubmed |
| pubmed-article:9925773 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9925773 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:9925773 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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