File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Two dimensional crowding effects on protein folding at interfaces observed by chiral vibrational sum frequency generation spectroscopy

TitleTwo dimensional crowding effects on protein folding at interfaces observed by chiral vibrational sum frequency generation spectroscopy
Authors
Issue Date2018
Citation
Physical Chemistry Chemical Physics, 2018, v. 20, n. 35, p. 22421-22426 How to Cite?
Abstract© the Owner Societies. The crowding effect is prevalent in cellular environments due to high concentrations of biomacromolecules. It can alter the structures and dynamics of proteins and thus impact protein functions. The crowding effect is important not only in 3-dimensional cytoplasm but also for a 2-dimensional (2D) cell surface due to the presence of membrane proteins and glycosylation of membrane proteins and phospholipids. These proteins and phospholipids-with limited translational degrees of freedom along the surface normal-are confined in 2D space. Although the crowding effect at interfaces has been studied by adding crowding agents to bulk solution, the 2D crowding effect remains largely unexplored. This is mostly due to challenges in controlling 2D crowding and synergistic use of physical methods for in situ protein characterization. To address these challenges, we applied chiral vibrational sum frequency generation (SFG) spectroscopy to probe the sp1 zinc finger (ZnF), a 31-amino acid protein, folding into a β-hairpin/α-helix (ββα) motif upon binding to Zn2+. We anchored ZnF at the air/water interface via covalent linkage of ZnF to palmitic acid and controlled 2D crowding by introducing neutral lipid as a spacer. We obtained chiral amide I SFG spectra upon addition of Zn2+ and/or spacer lipid. The chiral SFG spectra show that interfacial crowding in the absence of spacer lipid hinders ZnF from folding into the ββα structure even in the presence of Zn2+. The results establish a paradigm for future quantitative, systematic studies of interfacial crowding effects.
DescriptionAuthor version manuscript is available on the publisher website.
Persistent Identifierhttp://hdl.handle.net/10722/283656
ISSN
2023 Impact Factor: 2.9
2023 SCImago Journal Rankings: 0.721
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorLiu, Wei-
dc.contributor.authorFu, Li-
dc.contributor.authorWang, Zhuguang-
dc.contributor.authorSohrabpour, Zahra-
dc.contributor.authorLi, Xiaobai-
dc.contributor.authorLiu, Yuting-
dc.contributor.authorWang, Hong fei-
dc.contributor.authorYan, Elsa C.Y.-
dc.date.accessioned2020-07-03T08:07:55Z-
dc.date.available2020-07-03T08:07:55Z-
dc.date.issued2018-
dc.identifier.citationPhysical Chemistry Chemical Physics, 2018, v. 20, n. 35, p. 22421-22426-
dc.identifier.issn1463-9076-
dc.identifier.urihttp://hdl.handle.net/10722/283656-
dc.descriptionAuthor version manuscript is available on the publisher website.-
dc.description.abstract© the Owner Societies. The crowding effect is prevalent in cellular environments due to high concentrations of biomacromolecules. It can alter the structures and dynamics of proteins and thus impact protein functions. The crowding effect is important not only in 3-dimensional cytoplasm but also for a 2-dimensional (2D) cell surface due to the presence of membrane proteins and glycosylation of membrane proteins and phospholipids. These proteins and phospholipids-with limited translational degrees of freedom along the surface normal-are confined in 2D space. Although the crowding effect at interfaces has been studied by adding crowding agents to bulk solution, the 2D crowding effect remains largely unexplored. This is mostly due to challenges in controlling 2D crowding and synergistic use of physical methods for in situ protein characterization. To address these challenges, we applied chiral vibrational sum frequency generation (SFG) spectroscopy to probe the sp1 zinc finger (ZnF), a 31-amino acid protein, folding into a β-hairpin/α-helix (ββα) motif upon binding to Zn2+. We anchored ZnF at the air/water interface via covalent linkage of ZnF to palmitic acid and controlled 2D crowding by introducing neutral lipid as a spacer. We obtained chiral amide I SFG spectra upon addition of Zn2+ and/or spacer lipid. The chiral SFG spectra show that interfacial crowding in the absence of spacer lipid hinders ZnF from folding into the ββα structure even in the presence of Zn2+. The results establish a paradigm for future quantitative, systematic studies of interfacial crowding effects.-
dc.languageeng-
dc.relation.ispartofPhysical Chemistry Chemical Physics-
dc.titleTwo dimensional crowding effects on protein folding at interfaces observed by chiral vibrational sum frequency generation spectroscopy-
dc.typeArticle-
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1039/C7CP07061F-
dc.identifier.pmid30159555-
dc.identifier.scopuseid_2-s2.0-85053349617-
dc.identifier.volume20-
dc.identifier.issue35-
dc.identifier.spage22421-
dc.identifier.epage22426-
dc.identifier.isiWOS:000445220500001-
dc.identifier.issnl1463-9076-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats