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Robert G. Chapman

Researcher at National Research Council

Publications -  17
Citations -  4501

Robert G. Chapman is an academic researcher from National Research Council. The author has contributed to research in topics: Adsorption & Polyunsaturated fatty acid. The author has an hindex of 12, co-authored 17 publications receiving 4236 citations. Previous affiliations of Robert G. Chapman include Brigham and Women's Hospital & Harvard University.

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A Survey of Structure−Property Relationships of Surfaces that Resist the Adsorption of Protein

TL;DR: In this paper, the authors used surface plasmon resonance spectroscopy and self-assembled monolayers (SAMs) to determine the characteristics of functional groups that give surfaces the ability to resist the nonspecific adsorption of proteins from solution.
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Zwitterionic SAMs that Resist Nonspecific Adsorption of Protein from Aqueous Buffer

TL;DR: This paper describes the use of surface plasmon resonance spectroscopy and self-assembled monolayers (SAMs) of alkanethiols on gold to evaluate the ability of surfaces terminating in different combinations of charged groups to resist the nonspecific adsorption of proteins from aqueous buffer.
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Self-assembled monolayers that resist the adsorption of proteins and the adhesion of bacterial and mammalian cells

TL;DR: There seems to be little or no correlation between the adsorption of protein (fibrinogen and lysozyme) and the adhesion of cells.
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Surveying for Surfaces that Resist the Adsorption of Proteins

TL;DR: In this article, the authors describe an experimentally straightforward procedure for preparing and screening surfaces for their ability to resist the adsorption of proteins from solution, which is referred to as protein resistant surfaces.
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Polymeric Thin Films That Resist the Adsorption of Proteins and the Adhesion of Bacteria

TL;DR: In this article, the authors describe the design and preparation of thin polymeric films that resist the adsorption of proteins and the adhesion of bacteria to an extent comparable to, or better than, self-assembled monolayers (SAMs) that present tri(ethylene glycol) groups.