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

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Journal articles on the topic "Protein surfaces"

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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 (2019): 77–85. http://dx.doi.org/10.1093/protein/gzz033.

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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 pre
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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 (2004): 431–49. http://dx.doi.org/10.1142/s1469026804001392.

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

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

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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 (2018): 8352–57. http://dx.doi.org/10.1073/pnas.1800287115.

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

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Lehnfeld, J., Y. Dukashin, J. Mark, et al. "Saliva and Serum Protein Adsorption on Chemically Modified Silica Surfaces." Journal of Dental Research 100, no. 10 (2021): 1047–54. http://dx.doi.org/10.1177/00220345211022273.

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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 bi
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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 (2012): 2348–80. http://dx.doi.org/10.1098/rsta.2011.0484.

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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
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Wach, Jean-Yves, Barbora Malisova, Simone Bonazzi, et al. "Protein-Resistant Surfaces through Mild Dopamine Surface Functionalization." Chemistry - A European Journal 14, no. 34 (2008): 10579–84. http://dx.doi.org/10.1002/chem.200801134.

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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.

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Dissertations / Theses on the topic "Protein surfaces"

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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.

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

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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.

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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.

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

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

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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.

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

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

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Thesis (M. S.)--Materials Science and Engineering, Georgia Institute of Technology, 2008.<br>Committee Chair: Tsukruk, Vladimir; Committee Member: Kalaitzidou, Kyriaki; Committee Member: Valeria Milam.
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Frazier, Richard Andrew. "Macromolecular interactions at polysaccharide surfaces." Thesis, University of Nottingham, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.336946.

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Books on the topic "Protein surfaces"

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

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Eunice, Li-Chan, ed. Hydrophobic interactions in food systems. CRC Press, 1988.

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

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

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

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(Firm), Anatrace. Detergents and their uses in membrane protein science. Anatrace, 2007.

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

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

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

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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. Elsevier, 2001.

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Book chapters on the topic "Protein surfaces"

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

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

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

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

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

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

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

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

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

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

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Conference papers on the topic "Protein surfaces"

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Cotton, Therese M., Bernard Rospendowski, Vicki Schlegel, et al. "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.

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

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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.

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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.

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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.

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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 pre
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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.

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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.

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

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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.

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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
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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.

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Reports on the topic "Protein surfaces"

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

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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), 2000. http://dx.doi.org/10.2172/773875.

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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), 2004. http://dx.doi.org/10.2172/825532.

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

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

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

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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. Defense Technical Information Center, 2001. http://dx.doi.org/10.21236/ada389135.

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

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

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

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