Structural Changes in Barley Protein LTP1 Isoforms at Air-Water Interfaces
We use a coarse-grained model to study the conformational changes in two barley proteins, LTP1 and its ligand adduct isoform LTP1b, that result from their adsorption to the air-water interface. The model introduces the interface through hydropathy indices. We justify the model by all-atom simulation...
| Publié dans: | Langmuir : the ACS journal of surfaces and colloids. - 1985. - 33(2017), 19 vom: 16. Mai, Seite 4769-4780 |
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| Format: | Article en ligne |
| Langue: | English |
| Publié: |
2017
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| Accès à la collection: | Langmuir : the ACS journal of surfaces and colloids |
| Sujets: | Journal Article Research Support, Non-U.S. Gov't Carrier Proteins Gases Protein Isoforms Water 059QF0KO0R |
| Résumé: | We use a coarse-grained model to study the conformational changes in two barley proteins, LTP1 and its ligand adduct isoform LTP1b, that result from their adsorption to the air-water interface. The model introduces the interface through hydropathy indices. We justify the model by all-atom simulations. The choice of the proteins is motivated by making attempts to understand formation and stability of foam in beer. We demonstrate that both proteins flatten out at the interface and can make a continuous stabilizing and denser film. We show that the degree of the flattening depends on the protein (the layers of LTP1b should be denser than those of LTP1) and on the presence of glycation. It also depends on the number (≤4) of the disulfide bonds in the proteins. The geometry of the proteins is sensitive to the specificity of the absent bonds. We provide estimates of the volume of cavities of the proteins when away from the interface |
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| Description: | Date Completed 25.01.2019 Date Revised 25.01.2019 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1520-5827 |
| DOI: | 10.1021/acs.langmuir.7b00791 |