Relevant bibliographies by topics / Protein surfaces

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Protein surfaces'

Author: Grafiati
Published: 4 June 2021
Last updated: 15 February 2022

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Protein surfaces.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "Protein surfaces"

1

Khan, Mohammad Ashhar I., Ulrich Weininger, Sven Kjellström, Shashank Deep, and Mikael Akke. "Adsorption of unfolded Cu/Zn superoxide dismutase onto hydrophobic surfaces catalyzes its formation of amyloid fibrils." Protein Engineering, Design and Selection 32, no. 2 (February 2019): 77–85. http://dx.doi.org/10.1093/protein/gzz033.

Full text
Abstract:
Abstract Intracellular aggregates of superoxide dismutase 1 (SOD1) are associated with amyotrophic lateral sclerosis. In vivo, aggregation occurs in a complex and dense molecular environment with chemically heterogeneous surfaces. To investigate how SOD1 fibril formation is affected by surfaces, we used an in vitro model system enabling us to vary the molecular features of both SOD1 and the surfaces, as well as the surface area. We compared fibril formation in hydrophilic and hydrophobic sample wells, as a function of denaturant concentration and extraneous hydrophobic surface area. In the presence of hydrophobic surfaces, SOD1 unfolding promotes fibril nucleation. By contrast, in the presence of hydrophilic surfaces, increasing denaturant concentration retards the onset of fibril formation. We conclude that the mechanism of fibril formation depends on the surrounding surfaces and that the nucleating species might correspond to different conformational states of SOD1 depending on the nature of these surfaces.
APA, Harvard, Vancouver, ISO, and other styles
2

SHRESTHA, NRIPENDRA L., YOUHEI KAWAGUCHI, and TAKENAO OHKAWA. "SUMOMO: A PROTEIN SURFACE MOTIF MINING MODULE." International Journal of Computational Intelligence and Applications 04, no. 04 (December 2004): 431–49. http://dx.doi.org/10.1142/s1469026804001392.

Full text
Abstract:
Protein surface motifs, which can be defined as commonly appearing patterns of shape and physical properties in protein molecular surfaces, can be considered "possible active sites". We have developed a system for mining surface motifs: SUMOMO which consists of two phases: surface motif extraction and surface motif filtering. In the extraction phase, a given set of protein molecular surface data is divided into small surfaces called unit surfaces. After extracting several common unit surfaces as candidate motifs, they are repetitively merged into surface motifs. However, a large amount of surface motifs is extracted in this phase, making it difficult to distinguish whether the extracted motifs are significant to be considered active sites. Since active sites from proteins with a particular function have similar shape and physical properties, proteins can be classified based on similarity among local surfaces. Thus, in the filtering phase, local surfaces extracted from proteins of the same group are considered significant motifs, and the rest are filtered out. The proposed method was applied to discover surface motifs from 15 proteins belonging to four function groups. Motifs corresponding to all 4 known functional sites were recognised.
APA, Harvard, Vancouver, ISO, and other styles
3

Znamenskiy, Denis, Khan Le Tuan, Anne Poupon, Jacques Chomilier, and Jean-Paul Mornon. "β-Sheet modeling by helical surfaces." Protein Engineering, Design and Selection 13, no. 6 (June 2000): 407–12. http://dx.doi.org/10.1093/protein/13.6.407.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Connolly, Michael L. "Plotting protein surfaces." Journal of Molecular Graphics 4, no. 2 (June 1986): 93–96. http://dx.doi.org/10.1016/0263-7855(86)80004-2.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Kurnik, Martin, Gabriel Ortega, Philippe Dauphin-Ducharme, Hui Li, Amanda Caceres, and Kevin W. Plaxco. "Quantitative measurements of protein−surface interaction thermodynamics." Proceedings of the National Academy of Sciences 115, no. 33 (July 30, 2018): 8352–57. http://dx.doi.org/10.1073/pnas.1800287115.

Full text
Abstract:
Whereas proteins generally remain stable upon interaction with biological surfaces, they frequently unfold on and adhere to artificial surfaces. Understanding the physicochemical origins of this discrepancy would facilitate development of protein-based sensors and other technologies that require surfaces that do not compromise protein structure and function. To date, however, only a small number of such artificial surfaces have been reported, and the physics of why these surfaces support functional biomolecules while others do not has not been established. Thus motivated, we have developed an electrochemical approach to determining the folding free energy of proteins site-specifically attached to chemically well-defined, macroscopic surfaces. Comparison with the folding free energies seen in bulk solution then provides a quantitative measure of the extent to which surface interactions alter protein stability. As proof-of-principle, we have characterized the FynSH3 domain site-specifically attached to a hydroxyl-coated surface. Upon guanidinium chloride denaturation, the protein unfolds in a reversible, two-state manner with a free energy within 2 kJ/mol of the value seen in bulk solution. Assuming that excluded volume effects stabilize surface-attached proteins, this observation suggests there are countervening destabilizing interactions with the surface that, under these conditions, are similar in magnitude. Our technique constitutes an unprecedented experimental tool with which to answer long-standing questions regarding the molecular-scale origins of protein−surface interactions and to facilitate rational optimization of surface biocompatibility.
APA, Harvard, Vancouver, ISO, and other styles
6

Ban, Yih-En Andrew, Herbert Edelsbrunner, and Johannes Rudolph. "Interface surfaces for protein-protein complexes." Journal of the ACM 53, no. 3 (May 2006): 361–78. http://dx.doi.org/10.1145/1147954.1147957.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Lehnfeld, J., Y. Dukashin, J. Mark, G. D. White, S. Wu, V. Katzur, R. Müller, and S. Ruhl. "Saliva and Serum Protein Adsorption on Chemically Modified Silica Surfaces." Journal of Dental Research 100, no. 10 (June 22, 2021): 1047–54. http://dx.doi.org/10.1177/00220345211022273.

Full text
Abstract:
Biomaterials, once inserted in the oral cavity, become immediately covered by a layer of adsorbed proteins that consists mostly of salivary proteins but also of plasma proteins if the biomaterial is placed close to the gingival margin or if it becomes implanted into tissue and bone. It is often this protein layer, rather than the pristine biomaterial surface, that is subsequently encountered by colonizing bacteria or attaching tissue cells. Thus, to study this important initial protein adsorption from human saliva and serum and how it might be influenced through chemical modification of the biomaterial surface, we have measured the amount of protein adsorbed and analyzed the composition of the adsorbed protein layer using gel electrophoresis and western blotting. Here, we have developed an in vitro model system based on silica surfaces, chemically modified with 7 silane-based self-assembled monolayers that span a broad range of physicochemical properties, from hydrophilic to hydrophobic surfaces (water contact angles from 15° to 115°), low to high surface free energy (12 to 57 mN/m), and negative to positive surface charge (zeta potentials from –120 to +40 mV at physiologic pH). We found that the chemical surface functionalities exerted a substantial effect on the total amounts of proteins adsorbed; however, no linear correlation of the adsorbed amounts with the physicochemical surface parameters was observed. Only the adsorption behavior of a few singular protein components, from which physicochemical data are available, seems to follow physicochemical expectations. Examples are albumin in serum and lysozyme in saliva; in both, adsorption was favored on countercharged surfaces. We conclude from these findings that in complex biofluids such as saliva and serum, adsorption behavior is dominated by the overall protein-binding capacity of the surface rather than by specific physicochemical interactions of single protein entities with the surface.
APA, Harvard, Vancouver, ISO, and other styles
8

Schricker, Scott R., Manuel L. B. Palacio, and Bharat Bhushan. "Designing nanostructured block copolymer surfaces to control protein adhesion." Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences 370, no. 1967 (May 28, 2012): 2348–80. http://dx.doi.org/10.1098/rsta.2011.0484.

Full text
Abstract:
The profile and conformation of proteins that are adsorbed onto a polymeric biomaterial surface have a profound effect on its in vivo performance. Cells and tissue recognize the protein layer rather than directly interact with the surface. The chemistry and morphology of a polymer surface will govern the protein behaviour. So, by controlling the polymer surface, the biocompatibility can be regulated. Nanoscale surface features are known to affect the protein behaviour, and in this overview the nanostructure of self-assembled block copolymers will be harnessed to control protein behaviour. The nanostructure of a block copolymer can be controlled by manipulating the chemistry and arrangement of the blocks. Random, A–B and A–B–A block copolymers composed of methyl methacrylate copolymerized with either acrylic acid or 2-hydroxyethyl methacrylate will be explored. Using atomic force microscopy (AFM), the surface morphology of these block copolymers will be characterized. Further, AFM tips functionalized with proteins will measure the adhesion of that particular protein to polymer surfaces. In this manner, the influence of block copolymer morphology on protein adhesion can be measured. AFM tips functionalized with antibodies to fibronectin will determine how the surfaces will affect the conformation of fibronectin, an important parameter in evaluating surface biocompatibility.
APA, Harvard, Vancouver, ISO, and other styles
9

Wach, Jean-Yves, Barbora Malisova, Simone Bonazzi, Samuele Tosatti, Marcus Textor, Stefan Zürcher, and Karl Gademann. "Protein-Resistant Surfaces through Mild Dopamine Surface Functionalization." Chemistry - A European Journal 14, no. 34 (October 16, 2008): 10579–84. http://dx.doi.org/10.1002/chem.200801134.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Hato, Masakatsu, Masami Murata, and Takeshi Yoshida. "Surface forces between protein A adsorbed mica surfaces." Colloids and Surfaces A: Physicochemical and Engineering Aspects 109 (April 1996): 345–61. http://dx.doi.org/10.1016/0927-7757(95)03466-8.

Full text
APA, Harvard, Vancouver, ISO, and other styles
More sources

Dissertations / Theses on the topic "Protein surfaces"

1

Roach, Paul. "Measurement of surface-protein interactions on novel surfaces." Thesis, Nottingham Trent University, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.431900.

Full text
Abstract:
This thesis is concerned with the fundamental principles affecting protein adsorption. The effects of surface chemistry and topography on protein adsorption characteristics have been identified and quantified. Particular attention has been made to understand how the conformation of surface-bound proteins was affected by the surface onto which they adsorbed. Quartz crystal microbalance (QCM), UV-Vis spectroscopy and fluorometry were used to assess protein-surface affinity and amounts of protein adsorbed at surface saturation levels. Infrared spectroscopy was used to quantify protein conformational changes incurred upon adsorption. A fluorescent assay protocol was developed for use as an external calibration method for the quantification of adsorbed protein an d the results obtained were compared with QCM and an amido black protein assay of the same systems. Model experiments were performed using bovine fibrinogen (an elongated molecule) and albumin (a globular molecule) adsorbing onto flat hydrophilic (OH terminated) and hydrophobic (CH3 terminated) surfaces in the first instance, but later superhydrophilic and superhydrophobic surfaces were also studied. Surface curvature on the nano-scale was used to model topography, wherein protein molecules adsorbed onto spherical substrates (15-165 nm diameter) having chemically defined surfaces. Results obtained indicate that both proteins exhibit a less organised secondary structure upon adsorption onto hydrophobic compared to hydrophilic surfaces, with this effect being greatest for albumin. Adsorption rates and binding affinities were found to be higher on hydrophobic surfaces although the amounts adsorbed at saturation were lower. Supporting spectroscopic data suggests that proteins undergo surface induced deformation upon adsorption. Topography was shown to compound the effects of surface chemistry, with fibrinogen being more denatured on surfaces presenting high surface curvature whereas albumin was more denatured on larger substrates. These effects are most probably due to the differing size and shape of the proteins investigated. This study highlights the possibility of using tailor-made surfaces to influence binding rates and the conformation of bound proteins through protein-surface interactions. The data presented in this thesis demonstrates our ability to control protein adsorption characteristics through careful consideration of the underlying surface, which may facilitate the development and fabrication of materials / surface coatings with tailored bioactivity.
APA, Harvard, Vancouver, ISO, and other styles
2

Mathes, Johannes. "Protein Adsorption to Vial Surfaces." Diss., lmu, 2010. http://nbn-resolving.de/urn:nbn:de:bvb:19-121255.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Shi, Huaiqiu Galen. "Protein recognition of template imprinted polymer surfaces /." Thesis, Connect to this title online; UW restricted, 1999. http://hdl.handle.net/1773/8075.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Rosengren, Åsa. "Cell-protein-material interactions on bioceramics and model surfaces /." Uppsala : Acta Universitatis Upsaliensis : Univ.-bibl. [distributör], 2004. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-4688.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Gerstein, Mark. "Protein recognition : surfaces and conformational change." Thesis, University of Cambridge, 1992. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.282099.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Archambault, Jacques Gérard. "Protein adsorption to polyethylene oxide-grafted surfaces /." *McMaster only, 2002.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
7

McKavanagh, Fiona. "Measrement of protein interactions on tailored surfaces." Thesis, University of Ulster, 2010. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.526958.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Davidson, Katrina Ann. "Protein refolding via immobilisation on crystal surfaces." Thesis, University of Glasgow, 2008. http://theses.gla.ac.uk/345/.

Full text
Abstract:
Is it possible to find an easy, generic method for protein refolding? The preparation of functionally active protein molecules from the unfolded state can be a difficult task. Although there are many well-established techniques for protein refolding, such as dilution, dialysis, chromatography and others, in many instances these methods can be time consuming and inefficient. A rapid, inexpensive and simple method for protein folding is a much sought after technique. Proteins in the unfolded state (either inclusion bodies or unfolded by chemical or physical means) are generally solubilised in solutions containing urea or guanidine hydrochloride. The removal of these molecules from the protein environment is commonly utilised as a method for triggering refolding. A new method for the refolding of biomolecular species has been developed via the formation of Protein Coated Micro-crystals (PCMC). The formation of PCMC is a recently developed method for the immobilisation protein upon the surface of a watersoluble excipient (salt, amino acid or sugar) via a co-precipitation reaction in a water miscible organic solvent. These proteins can then be used as immobilised biocatalysts in both the aqueous and organic phase. In the immobilisation of unfolded, solubilised protein, the solubilising agents (e.g. urea or guanidine hydrochloride) are removed from the protein environment as they are soluble in the organic phase. The removal of these molecules initiates protein folding during the coprecipitation process. In the course of this project, a number of proteins were studied in order to observe their behaviour in this immobilisation and simultaneous folding process. Lysozyme was utilised as it is an enzyme which is relatively simple to refold from the chemically unfolded state by conventional methods such as dilution. Upon immobilisation of lysozyme from the chemically unfolded state, up to 92% of the activity of the native protein was regained. The enzyme lipase, which is notoriously difficult to fold, was also used to determine the efficiency of this method under more challenging conditions. Lipase immobilised from the chemically unfolded state was seen to regain up to 36 % of the activity of the native protein.
APA, Harvard, Vancouver, ISO, and other styles
9

Bergman, Kathryn N. "Biomineralization of inorganic nanostructures using protein surfaces." Thesis, Atlanta, Ga. : Georgia Institute of Technology, 2008. http://hdl.handle.net/1853/22674.

Full text
Abstract:
Thesis (M. S.)--Materials Science and Engineering, Georgia Institute of Technology, 2008.
Committee Chair: Tsukruk, Vladimir; Committee Member: Kalaitzidou, Kyriaki; Committee Member: Valeria Milam.
APA, Harvard, Vancouver, ISO, and other styles
10

Frazier, Richard Andrew. "Macromolecular interactions at polysaccharide surfaces." Thesis, University of Nottingham, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.336946.

Full text
APA, Harvard, Vancouver, ISO, and other styles
More sources

Books on the topic "Protein surfaces"

1

Puleo, David A. Biological interactions on materials surfaces: Understanding and controlling protein, cell, and tissue responses. Dordrecht: Springer, 2009.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
2

Eunice, Li-Chan, ed. Hydrophobic interactions in food systems. Boca Raton, Fla: CRC Press, 1988.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
3

Chen, Guodong. Characterization of Protein Therapeutics using Mass Spectrometry. Boston, MA: Springer US, 2013.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
4

Giralt, Ernest, Mark W. Peczuh, and Xavier Salvatella, eds. Protein Surface Recognition. Chichester, UK: John Wiley & Sons, Ltd, 2010. http://dx.doi.org/10.1002/9780470972137.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Giralt, Ernest, Mark Peczuh, and Xavier Salvatella. Protein surface recognition: Approaches for drug discovery. Chichester, West Sussex: John Wiley & Sons, 2011.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
6

(Firm), Anatrace. Detergents and their uses in membrane protein science. Maumee, OH (434 W. Duseel Dr., Maumee 43537): Anatrace, 2007.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
7

Ladd, Mark. Structure Determination by X-ray Crystallography: Analysis by X-rays and Neutrons. 5th ed. Boston, MA: Springer US, 2013.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
8

Mandeep. Characterization and plasma protein binding studies of surface modified polyethersulfone. Ottawa: National Library of Canada, 2001.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
9

Izmaĭlova, V. N. Poverkhnostnye i͡a︡vlenii͡a︡ v belkovykh sistemakh. Moskva: "Khimii͡a︡", 1988.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
10

Shigehiko, Mizutani, and Turner A. J. 1947-, eds. Cell-surface aminopeptidases: Basic and clinical aspects : proceedings of the 'International Conference on Cell-Surface Aminopeptidases', held in Nagoya, Japan, on 15-17 August, 2000. Amsterdam: Elsevier, 2001.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
More sources

Book chapters on the topic "Protein surfaces"

1

Warkentin, Peter H., Ingemar Lundström, and Pentti Tengvall. "Protein—Protein Interactions Affecting Proteins at Surfaces." In ACS Symposium Series, 163–80. Washington, DC: American Chemical Society, 1995. http://dx.doi.org/10.1021/bk-1995-0602.ch012.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Jung, Woongsic, Young-Pil Kim, and EonSeon Jin. "Antifreeze Protein-Covered Surfaces." In Antifreeze Proteins Volume 2, 307–26. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-41948-6_13.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Phillips, Jeff M., Johannes Rudolph, and Pankaj K. Agarwal. "Segmenting Motifs in Protein-Protein Interface Surfaces." In Lecture Notes in Computer Science, 207–18. Berlin, Heidelberg: Springer Berlin Heidelberg, 2006. http://dx.doi.org/10.1007/11851561_20.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Schmidt, David Richard, Heather Waldeck, and Weiyuan John Kao. "Protein Adsorption to Biomaterials." In Biological Interactions on Materials Surfaces, 1–18. New York, NY: Springer US, 2009. http://dx.doi.org/10.1007/978-0-387-98161-1_1.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Fuller, K. L., and S. G. Roscoe. "Surface adsorption of dairy proteins: Fouling of model surfaces." In Protein Structure-Function Relationships in Foods, 143–62. Boston, MA: Springer US, 1994. http://dx.doi.org/10.1007/978-1-4615-2670-4_7.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

McKenzie, Janice L., and Thomas J. Webster. "Protein Interactions at Material Surfaces." In Biomedical Materials, 215–37. Boston, MA: Springer US, 2009. http://dx.doi.org/10.1007/978-0-387-84872-3_8.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

McKenzie, Janice L., Thomas J. Webster, and J. L. McKenzie. "Protein Interactions at Material Surfaces." In Biomedical Materials, 399–422. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-49206-9_12.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Li, Y. W., T. Wüst, and D. P. Landau. "Biologically Inspired Surface Physics: The HP Protein Model." In Nanophenomena at Surfaces, 169–83. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-16510-8_7.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Cafiso, David S. "Structure and Interactions of C2 Domains at Membrane Surfaces." In Protein-Lipid Interactions, 403–22. Weinheim, FRG: Wiley-VCH Verlag GmbH & Co. KGaA, 2006. http://dx.doi.org/10.1002/3527606769.ch16.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Mora, Maria F., Jennifer L. Wehmeyer, Ron Synowicki, and Carlos D. Garcia. "Investigating Protein Adsorption via Spectroscopic Ellipsometry." In Biological Interactions on Materials Surfaces, 19–41. New York, NY: Springer US, 2009. http://dx.doi.org/10.1007/978-0-387-98161-1_2.

Full text
APA, Harvard, Vancouver, ISO, and other styles

Conference papers on the topic "Protein surfaces"

1

Cotton, Therese M., Bernard Rospendowski, Vicki Schlegel, Robert A. Uphaus, Danli L. Wang, Lars Eng, and Marion T. Stankovich. "Spectroscopy of proteins on surfaces: implications for protein orientation and protein-protein interactions." In Moscow - DL tentative, edited by Sergei A. Akhmanov and Marina Y. Poroshina. SPIE, 1991. http://dx.doi.org/10.1117/12.57297.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Ban, Yih-En Andrew, Herbert Edelsbrunner, and Johannes Rudolph. "Interface surfaces for protein-protein complexes." In the eighth annual international conference. New York, New York, USA: ACM Press, 2004. http://dx.doi.org/10.1145/974614.974642.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Baxter, R., A. Jones, and H. Baxter. "Quantification of protein contamination on surfaces." In 2012 IEEE 39th International Conference on Plasma Sciences (ICOPS). IEEE, 2012. http://dx.doi.org/10.1109/plasma.2012.6383563.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Cristea, Paul Dan, Rodica Tuduce, Octavian Arsene, and Dan V. Nicolau. "Functional nanoscale imaging of protein surfaces." In SPIE BiOS, edited by Alexander N. Cartwright and Dan V. Nicolau. SPIE, 2011. http://dx.doi.org/10.1117/12.888816.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Adams, G. A., and C. Hallée. "THROMBOSPONDIN ADSORPTION AND PLATELET ADHESION TO SURFACES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643589.

Full text
Abstract:
Recent research into cell adhesion has focused on a tripeptide sequence arg-gly-asp (RGD) that is common to a number of cytoadhesive proteins such as von Willebrand factor, fibronectin and fibrinogen. We have previously reported that thrombospondin (TSP) inhibited platelet adhesion to RGD proteins. On further purification of TSP, the inhibitory activity separated away from the TSP. In this report, we demonstate that TSP adsorbs to surfaces and promotes platelet adhesion and thus may belong to this family of cytoadhesins. TSP was purified by heparin affinity chromatography, ammonium sulfate precipitation and sucrose gradient ultracentrifugation. Final preparations were free of TSP aggregates and gave one band on SDS-PAGE. Washed human platelets were radiolabelled, combined with red blood cells and perfused through protein-coated glass or polyethylene (PE) tubes for 7 mins. at a shear rate of 100 s™1. TSP supported platelet adhesion to the same level as fibrinogen (FG), but less than collagen. Platelets were spread but no thrombi were present on the TSP or FG-coated tubes while thrombi formed on collagen-coated tubes. Levels of adsorption were similar for purified solutions of radioiodinated FG or TSP on both glass and PE surfaces. The competitive interactions between these proteins during adsorption to surfaces indicated at equimolar amounts the TSP and FG both deposited on the surface but as FG:TSP ratio increased FG was preferentially adsorbed. These results indicate that TSP is a cytoadhesive protein for platelets when it is adsorbed to surfaces. Thus, the release of TSP from platelets may promote haemostasis or thrombogenesis.(supported by Ontario Heart Foundation, Canada)
APA, Harvard, Vancouver, ISO, and other styles
6

Han, Z. J., M. Shakerzadeh, B. K. Tay, and C. M. Tan. "Protein immobilization on nanostructured surfaces with different wettability." In 2010 IEEE 3rd International Nanoelectronics Conference (INEC). IEEE, 2010. http://dx.doi.org/10.1109/inec.2010.5424833.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Cristea, Paul D., Octavian Arsene, Rodica Tuduce, and Dan V. Nicolau. "Hydrophobicity and charge nanoscale imaging of protein surfaces." In SPIE BiOS, edited by Alexander N. Cartwright and Dan V. Nicolau. SPIE, 2012. http://dx.doi.org/10.1117/12.928342.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Daberdaku, Sebastian. "Parallel Computation of Voxelised Protein Surfaces with OpenMP." In the 6th International Workshop. New York, New York, USA: ACM Press, 2018. http://dx.doi.org/10.1145/3235830.3235833.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Kim, Sungwon S., Tom T. Huang, Timothy S. Fisher, and Michael R. Ladisch. "Effects of Carbon Nanotube Structure on Protein Adsorption." In ASME 2005 International Mechanical Engineering Congress and Exposition. ASMEDC, 2005. http://dx.doi.org/10.1115/imece2005-81395.

Full text
Abstract:
Outstanding transport characteristics and high surface-to-volume ratios are several advantages that carbon nanotubes possess that make them attractive candidates for protein immobilization matrices in biosensor applications. A further advantage of using carbon nanotubes is that their structure (e.g., diameter, length, density) can potentially be controlled during synthesis. In the present study, the effects of carbon nanotube structure on enzyme immobilization onto carbon nanotube arrays are investigated. Bovine serum albumin (BSA) serves as both a blocking agent for prevention of nonspecific adsorption and as a support for anchoring bioreceptors. BSA, a globular protein having a 4 to 6 nm characteristic dimension, is stably adsorbed through mechanisms that involve hydrophobic interactions between surfaces presented by the carbon nanotubes and the spacing between the nanotubes with the protein. Protein adsorption is confirmed by fluorescence microscopy of surfaces that have been exposed to fluourescein isothiocyanate (FITC) labeled BSA. The adsorption of biotinylated BSA can be used, through a sandwich immobilization scheme, to provide an anchor for streptavidin, which in turn has at least one other adsorption site that is specific for other biotinylated proteins such as glucose oxidase that would form a biorecognition or catalytic element in a functional biosensor. Correlation between carbon nanotube structure and protein adsorption at the nano-bio interface could eventually lead to growth conditions that yield carbon nanotubes for biosensor applications with optimal protein adsorption characteristics.
APA, Harvard, Vancouver, ISO, and other styles
10

Agarwal, Ashutosh, Parag Katira, and Henry Hess. "Quantifying and understanding protein adsorption to non-fouling surfaces." In 2010 36th Annual Northeast Bioengineering Conference. IEEE, 2010. http://dx.doi.org/10.1109/nebc.2010.5458217.

Full text
APA, Harvard, Vancouver, ISO, and other styles

Reports on the topic "Protein surfaces"

1

Gilpin, Roger K. Development of Novel Switchable Protein Surfaces. Fort Belvoir, VA: Defense Technical Information Center, December 1993. http://dx.doi.org/10.21236/ada275510.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Follstaedt, S. C., D. K. Cheung, P. L. Gourley, and D. Y. Sasaki. Protein Adhesion on SAM Coated Semiconductor Wafers: Hydrophobic versus Hydrophilic Surfaces. Office of Scientific and Technical Information (OSTI), December 2000. http://dx.doi.org/10.2172/773875.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Koffas, Telly Stelianos. Characterization of the molecular structure and mechanical properties of polymer surfaces and protein/polymer interfaces by sum frequency generation vibrational spectroscopy and atomic force microscopy. Office of Scientific and Technical Information (OSTI), January 2004. http://dx.doi.org/10.2172/825532.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Webb, Lauren J. Electrostatic Control of Protein-Surface Interactions. Fort Belvoir, VA: Defense Technical Information Center, October 2013. http://dx.doi.org/10.21236/ada597412.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Smith, H. G. Surface-Bound Membrane-Mimetic Assemblies: Electrostatic Attributes of Integral Membrane Proteins. Fort Belvoir, VA: Defense Technical Information Center, October 1988. http://dx.doi.org/10.21236/ada204381.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Smith, H. G. Surface-Bound Membrane-Mimetic Assemblies: Electrostatic Attributes of Integral Membrane Proteins. Fort Belvoir, VA: Defense Technical Information Center, June 1991. http://dx.doi.org/10.21236/ada237229.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Geesey, Gill G., Peter A. Suci, Peter R. Griffiths, and Georges Belfort. Characterization of Molecular Interactions of Mytilus edulis Foot Proteins on Model Hydrated Surfaces. Fort Belvoir, VA: Defense Technical Information Center, February 2001. http://dx.doi.org/10.21236/ada389135.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Drescher, Charles. Targeting Cell Surface Proteins in Molecular Photoacoustic Imaging to Detect Ovarian Cancer Early. Fort Belvoir, VA: Defense Technical Information Center, July 2012. http://dx.doi.org/10.21236/ada567976.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Drescher, Charles W. Targeting Cell Surface Proteins in Molecular Photoacoustic Imaging to Detect Ovarian Cancer Early. Fort Belvoir, VA: Defense Technical Information Center, July 2013. http://dx.doi.org/10.21236/ada591911.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Drescher, Charles W. Targeting Cell Surface Proteins in Molecular Photoacoustic Imaging to Detect Ovarian Cancer Early. Fort Belvoir, VA: Defense Technical Information Center, July 2011. http://dx.doi.org/10.21236/ada553529.

Full text
APA, Harvard, Vancouver, ISO, and other styles
You might also be interested in the extended bibliographies on the topic 'Protein surfaces' for particular source types:
Journal articles Dissertations / Theses Books
We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!

To the bibliography