Protein assemblies can accommodate a variety of organic, inorganic and biological molecules such as small proteins and peptides and have been used in development of subunit vaccines via display parts of viral pathogens or antigens.Next Article in Journal Dermal Drivers of Injury-Induced Inflammation: Contribution of Adipocytes and Fibroblasts.
Next Article in Special Issue pH-Responsive Self-Assembly of Designer Aromatic Peptide Amphiphiles and Enzymatic Post-Modification of Assembled Structures. Previous Article in Journal Effect of Hofmeister Ions on Transport Properties of Aqueous Solutions of Sodium Hyaluronate. Previous Article in Special Issue Synthesis and Self-Assembly Properties of Bola-Amphiphilic Glycosylated Lipopeptide-Type Supramolecular Hydrogels Showing Colour Changes Along with GelSol Transition. Please note that many of the page functionalities wont work as expected without javascript enabled. European Journal of Investigation in Health, Psychology and Education (EJIHPE). International Journal of Environmental Research and Public Health (IJERPH). International Journal of Turbomachinery, Propulsion and Power (IJTPP). Journal of Open Innovation: Technology, Market, and Complexity (JOItmC). Journal of Otorhinolaryngology, Hearing and Balance Medicine (OHBM). Journal of Theoretical and Applied Electronic Commerce Research (JTAER). Find support for a specific problem in the support section of our website. Please let us know what you think of our products and services. Visit our dedicated information section to learn more about MDPI. The Versatile Manipulations of Self-Assembled Proteins in Vaccine Design. Received: 22 January 2021 Revised: 6 February 2021 Accepted: 11 February 2021 Published: 16 February 2021. ![]() Copyright (2018) American Chemical Society. Abbreviations: E, exon; PRD: protein rich domain; M: microtubule-binding domain. Reproduced with permission from Springer Nature (Creative Commons Attribution 4.0 International License) 16. Modified from 71. Reprinted with permission from American Association for the Advancement of Science (AAAS). The utilization of I53-50 as a carrier for respiratory syncytial virus antigen (DS-Cav1) conjugation; and ( c ) HIV-1 antigen (BG505 SOSIP) conjugation with negative stain electron microscopy (EM) images on the right side, respectively. The foldon domain at the C-terminus is presented in red with dimensions of 2.7 2.6 nm. The structure was rebuilt by PyMOL. Reprinted from 103, copyright (2008), with permission from Elsevier. Protein assemblies provide unique structural features which make them useful as carrier molecules in biomedical and chemical science.
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