Skip to main content

Dataset / Data from: New insights into cation-driven protein adsorption to the air-water interface …

Have a question about this item?

Item information. View source record on contributor's website.

Title
Data from: New insights into cation-driven protein adsorption to the air-water interface through infrared reflection studies of bovine serum albumin
Creator
Allen, Heather C
Enders, Abigail A
Date Created and/or Issued
Time period of project: 2021 to 2023
Contributing Institution
UC San Diego, Research Data Curation Program
Collection
Center for Aerosol Impacts on Chemistry of the Environment (CAICE)
Rights Information
Under copyright
Constraint(s) on Use: This work is protected by the U.S. Copyright Law (Title 17, U.S.C.). Use of this work beyond that allowed by "fair use" or any license applied to this work requires written permission of the copyright holder(s). Responsibility for obtaining permissions and any use and distribution of this work rests exclusively with the user and not the UC San Diego Library. Inquiries can be made to the UC San Diego Library program having custody of the work.
Use: This work is available from the UC San Diego Library. This digital copy of the work is intended to support research, teaching, and private study.
Rights Holder and Contact
UC Regents
Description
Publication abstract: The chemistry and structure of the air-ocean interface modulates biogeochemical processes between the ocean and atmosphere and therefore impacts sea spray aerosol properties, cloud and ice nucleation, and therefore climate. Protein macromolecules are enriched in the sea surface microlayer and have complex adsorption properties due to the unique molecular balance of hydrophobicity and hydrophilicity. Bovine serum albumin was used as a model protein to investigate the dynamic surface behavior of proteins under several variable conditions including solution ionic strength, temperature, and the presence of a fatty acid monolayer at the air-water interface. Key vibrational modes of bovine serum albumin are examined via infrared reflectance-absorbance spectroscopy, a specular reflection method that ratios out the solution phase and highlights the aqueous surface, to determine, at a molecular level, the surface structural changes and factors affecting adsorption to the solution surface. Amide band reflection absorption intensities reveal the extent of protein adsorption under each set of conditions. Studies revealed nuanced behavior of protein adsorption strongly impacted by ocean relevant sodium concentrations, and somewhat surprising, the adsorption was minimally impacted by divalent cations. The interfacial chemistry and properties are of interest because ocean surface biogeochemistry remains elusive and increased understanding of the surface in a controlled setting will help guide ocean and climate modeling.
Research Data Curation Program, UC San Diego, La Jolla, 92093-0175 (https://lib.ucsd.edu/rdcp)
Enders, Abigail A.; Clark, Jessica B.; Elliott, Scott M.; Allen, Heather C. (2023). Data from: New insights into cation-driven protein adsorption to the air-water interface through infrared reflection studies of bovine serum albumin. In Center for Aerosol Impacts on Chemistry of the Environment (CAICE) Collection. UC San Diego Library Digital Collections. https://doi.org/10.6075/J0D79BKR
Type
dataset
Identifier
ark:/20775/bb25704322
Language
English
Subject
Temperature
Protein
Surface adsorption
Ionic strength

About the collections in Calisphere

Learn more about the collections in Calisphere. View our statement on digital primary resources.

Copyright, permissions, and use

If you're wondering about permissions and what you can do with this item, a good starting point is the "rights information" on this page. See our terms of use for more tips.

Share your story

Has Calisphere helped you advance your research, complete a project, or find something meaningful? We'd love to hear about it; please send us a message.

Explore related content on Calisphere: