Investigation into the binding of dyes within protein crystals.
Identifieur interne : 000055 ( Main/Curation ); précédent : 000054; suivant : 000056Investigation into the binding of dyes within protein crystals.
Auteurs : Alexander Mcpherson [États-Unis] ; Steven B. Larson [États-Unis]Source :
- Acta crystallographica. Section F, Structural biology communications [ 2053-230X ] ; 2018.
Descripteurs français
- KwdFr :
- Agents colorants (composition chimique), Animaux (MeSH), Benzamidines (composition chimique), Bovins (MeSH), Coloration et marquage (méthodes), Cristallisation (MeSH), Cristallographie aux rayons X (MeSH), Liaison aux protéines (MeSH), Lysozyme (composition chimique), Modèles moléculaires (MeSH), Motifs et domaines d'intéraction protéique (MeSH), Poulets (MeSH), Protéines végétales (composition chimique), Sites de fixation (MeSH), Structure secondaire des protéines (MeSH), Trypsine (composition chimique), Virus satellite de la mosaïque du tabac (composition chimique).
- MESH :
- composition chimique : Agents colorants, Benzamidines, Lysozyme, Protéines végétales, Trypsine, Virus satellite de la mosaïque du tabac.
- méthodes : Coloration et marquage.
- Animaux, Bovins, Cristallisation, Cristallographie aux rayons X, Liaison aux protéines, Modèles moléculaires, Motifs et domaines d'intéraction protéique, Poulets, Sites de fixation, Structure secondaire des protéines.
English descriptors
- KwdEn :
- Animals (MeSH), Benzamidines (chemistry), Binding Sites (MeSH), Cattle (MeSH), Chickens (MeSH), Coloring Agents (chemistry), Crystallization (MeSH), Crystallography, X-Ray (MeSH), Models, Molecular (MeSH), Muramidase (chemistry), Plant Proteins (chemistry), Protein Binding (MeSH), Protein Interaction Domains and Motifs (MeSH), Protein Structure, Secondary (MeSH), Staining and Labeling (methods), Tobacco mosaic satellite virus (chemistry), Trypsin (chemistry).
- MESH :
- chemical , chemistry : Benzamidines, Coloring Agents, Muramidase, Plant Proteins, Trypsin.
- chemistry : Tobacco mosaic satellite virus.
- methods : Staining and Labeling.
- Animals, Binding Sites, Cattle, Chickens, Crystallization, Crystallography, X-Ray, Models, Molecular, Protein Binding, Protein Interaction Domains and Motifs, Protein Structure, Secondary.
Abstract
It was found that the crystals of at least a dozen different proteins could be thoroughly stained to an intense color with a panel of dyes. Many, if not most, of the stained protein crystals retained the dyes almost indefinitely when placed in large volumes of dye-free mother liquor. Dialysis experiments showed that most of the dyes that were retained in crystals also bound to the protein when free in solution; less frequently, some dyes bound only in the crystal. The experiments indicated a strong association of the dyes with the proteins. Four protein crystals were investigated by X-ray diffraction to ascertain the mode of binding. These were crystals of lysozyme, thaumatin, trypsin inhibited with benzamidine and satellite tobacco mosaic virus. In 30 X-ray analyses of protein crystal-dye complexes, in only three difference Fourier maps was any difference electron density present that was consistent with the binding of dye molecules, and even in these three cases (thaumatin plus thioflavin T, xylene cyanol and m-cresol purple) the amount of dye observed was inadequate to explain the intense color of the crystals. It was concluded that the dye molecules, which are clearly inside the crystals, are disordered but are paradoxically tightly bound to the protein. It is speculated that the dyes, which exhibit large hydrophobic cores and peripheral charged groups, may interact with the crystalline proteins in the manner of conventional detergents.
DOI: 10.1107/S2053230X18010300
PubMed: 30198893
PubMed Central: PMC6130428
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Many, if not most, of the stained protein crystals retained the dyes almost indefinitely when placed in large volumes of dye-free mother liquor. Dialysis experiments showed that most of the dyes that were retained in crystals also bound to the protein when free in solution; less frequently, some dyes bound only in the crystal. The experiments indicated a strong association of the dyes with the proteins. Four protein crystals were investigated by X-ray diffraction to ascertain the mode of binding. These were crystals of lysozyme, thaumatin, trypsin inhibited with benzamidine and satellite tobacco mosaic virus. In 30 X-ray analyses of protein crystal-dye complexes, in only three difference Fourier maps was any difference electron density present that was consistent with the binding of dye molecules, and even in these three cases (thaumatin plus thioflavin T, xylene cyanol and m-cresol purple) the amount of dye observed was inadequate to explain the intense color of the crystals. It was concluded that the dye molecules, which are clearly inside the crystals, are disordered but are paradoxically tightly bound to the protein. It is speculated that the dyes, which exhibit large hydrophobic cores and peripheral charged groups, may interact with the crystalline proteins in the manner of conventional detergents.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30198893</PMID><DateCompleted><Year>2018</Year><Month>12</Month><Day>11</Day></DateCompleted><DateRevised><Year>2020</Year><Month>09</Month><Day>01</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">2053-230X</ISSN><JournalIssue CitedMedium="Internet"><Volume>74</Volume><Issue>Pt 9</Issue><PubDate><Year>2018</Year><Month>Sep</Month><Day>01</Day></PubDate></JournalIssue><Title>Acta crystallographica. 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Four protein crystals were investigated by X-ray diffraction to ascertain the mode of binding. These were crystals of lysozyme, thaumatin, trypsin inhibited with benzamidine and satellite tobacco mosaic virus. In 30 X-ray analyses of protein crystal-dye complexes, in only three difference Fourier maps was any difference electron density present that was consistent with the binding of dye molecules, and even in these three cases (thaumatin plus thioflavin T, xylene cyanol and m-cresol purple) the amount of dye observed was inadequate to explain the intense color of the crystals. It was concluded that the dye molecules, which are clearly inside the crystals, are disordered but are paradoxically tightly bound to the protein. It is speculated that the dyes, which exhibit large hydrophobic cores and peripheral charged groups, may interact with the crystalline proteins in the manner of conventional detergents.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>McPherson</LastName><ForeName>Alexander</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Molecular Biology and Biochemistry, University of California Irvine, 560 Steinhaus Hall, Irvine, CA 92697-3900, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Larson</LastName><ForeName>Steven B</ForeName><Initials>SB</Initials><Identifier Source="ORCID">0000-0002-7681-8445</Identifier><AffiliationInfo><Affiliation>Molecular Biology and Biochemistry, University of California Irvine, 560 Steinhaus Hall, Irvine, CA 92697-3900, USA.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal 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