ArticleBiophysical journal2009
Ranaspumin-2: structure and function of a surfactant protein from the foam nests of a tropical frog.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
18 citing papers in PubMed, 51 citations in OpenAlex.
- Foam fractionation Tags (F-Tags) enabling surfactant-free, activity-preserving recovery of enzymes.Applied microbiology and biotechnology · 2024Article
- Neotropical Frog Foam Nest's Microbiomes.Microorganisms · 2023Article
- Genetically engineered materials: Proteins and beyond.Science China. Chemistry · 2022Review
- Frog nest foams exhibit pharmaceutical foam-like properties.Royal Society open science · 2021Article
- Transcriptomic analysis of differentially expressed genes in the oviduct of Rhacophorus omeimontis provides insights into foam nest construction.BMC genomics · 2019Article
- Valorization of papaya fruit waste through low-cost fractionation and microbial conversion of both juice and seed lipids.RSC advances · 2018Article
- Frog foams and natural protein surfactants.Colloids and surfaces. A, Physicochemical and engineering aspects · 2017Article
- EHD2 restrains dynamics of caveolae by an ATP-dependent, membrane-bound, open conformation.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- The Conformation of Interfacially Adsorbed Ranaspumin-2 Is an Arrested State on the Unfolding Pathway.Biophysical journal · 2016Article
- The Diverse Structures and Functions of Surfactant Proteins.Trends in biochemical sciences · 2016Review
- Recent Progress in Advanced Nanobiological Materials for Energy and Environmental Applications.Materials (Basel, Switzerland) · 2013Review
- The structure of latherin, a surfactant allergen protein from horse sweat and saliva.Journal of the Royal Society, Interface · 2013Article
- Crystallization and preliminary X-ray diffraction of the surfactant protein Lv-ranaspumin from the frog Leptodactylus vastus.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
- Biofoams and natural protein surfactants.Biophysical chemistry · 2010Review
- Building a home from foam--túngara frog foam nest architecture and three-phase construction process.Biology letters · 2010Article
- Latherin: a surfactant protein of horse sweat and saliva.PloS one · 2009Article
- Developmental diversity of amphibians.Wiley interdisciplinary reviews. Developmental biologyReview
- Aqueous solubilization of C60 fullerene by natural protein surfactants, latherin and ranaspumin-2.Biophysical chemistryArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Ranaspumin-2 (Rsn-2) is a monomeric, 11 kDa surfactant protein identified as one of the major foam nest components of the túngara frog (Engystomops pustulosus), with an amino acid sequence unlike any other protein described so far. We report here on its structure in solution as determined by high-resolution NMR analysis, together with investigations of its conformation and packing at the air-water interface using a combination of infrared and neutron reflectivity techniques. Despite the lack of any significant sequence similarity, Rsn-2 in solution adopts a compact globular fold characteristic of the cystatin family, comprising a single helix over a four-stranded sheet, in a motif not previously associated with surfactant activity. The NMR structure of Rsn-2 shows no obvious amphiphilicity that might be anticipated for a surfactant protein. This suggests that it must undergo a significant conformational change when incorporated into the air-water interface that may involve a hinge-bending, clamshell opening of the separate helix and sheet segments to expose hydrophobic faces to air while maintaining the highly polar surfaces in contact with the underlying water layer. This model is supported by direct observation of the relative orientations of secondary structure elements at the interface by infrared reflection absorption spectroscopy, and by protein packing densities determined from neutron reflectivity profiles.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.