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Adding Function to Protein Scaffolds. / Webster, Kyle; Sasso, Luigi; Domigan, Laura J.

Protein Nanotechnology: Protocols, Instrumentation, and Applications. ed. / Juliet A. Gerrard; Laura J. Domigan. New York, NY, USA : Springer, 2020. p. 119-147 (Methods in Molecular Biology; Vol. 2073).

Research output: Chapter in Book/Report/Conference proceedingChapterScientificpeer-review

Harvard

Webster, K, Sasso, L & Domigan, LJ 2020, Adding Function to Protein Scaffolds. in JA Gerrard & LJ Domigan (eds), Protein Nanotechnology: Protocols, Instrumentation, and Applications. Methods in Molecular Biology, vol. 2073, Springer, New York, NY, USA, pp. 119-147. https://doi.org/10.1007/978-1-4939-9869-2_8

APA

Webster, K., Sasso, L., & Domigan, L. J. (2020). Adding Function to Protein Scaffolds. In J. A. Gerrard, & L. J. Domigan (Eds.), Protein Nanotechnology: Protocols, Instrumentation, and Applications (pp. 119-147). (Methods in Molecular Biology; Vol. 2073). New York, NY, USA: Springer. https://doi.org/10.1007/978-1-4939-9869-2_8

Vancouver

Webster K, Sasso L, Domigan LJ. Adding Function to Protein Scaffolds. In Gerrard JA, Domigan LJ, editors, Protein Nanotechnology: Protocols, Instrumentation, and Applications. New York, NY, USA: Springer. 2020. p. 119-147. (Methods in Molecular Biology). https://doi.org/10.1007/978-1-4939-9869-2_8

Author

Webster, Kyle ; Sasso, Luigi ; Domigan, Laura J. / Adding Function to Protein Scaffolds. Protein Nanotechnology: Protocols, Instrumentation, and Applications. editor / Juliet A. Gerrard ; Laura J. Domigan. New York, NY, USA : Springer, 2020. pp. 119-147 (Methods in Molecular Biology).

BibTeX

@inbook{d015de980d674d2b891ae147b04d17f9,
title = "Adding Function to Protein Scaffolds",
abstract = "Biological systems often outperform artificial ones in ordering, assembly, and diversity of structure at the nanoscale. Proteins are particularly remarkable in this context. Through oligomerization, protein monomers assemble on multiple length scales, into larger and more complex structures such as viral capsids, filaments, and regulatory complexes. It is this structural diversity that makes proteins attractive candidates for use as functionalizable scaffolds. Well-established protein structure databases such as the protein data bank (PDB) allow researchers to search for a structure that fits their requirements, allowing them access to shapes and assembly mechanisms that would otherwise be difficult to achieve. Then, by employing functionalization techniques to conjugate artificial or biological molecules to their protein scaffold of choice, researchers can access chemistries beyond the limits of the 20 commonly occurring natural amino acids. Additionally, proteins, with a few exceptions, operate at physiological pH and temperature, making them ideal for medical applications and/or low-cost manufacture. Additionally, proteins sourced from extremophiles such as Thermus aquaticus (a bacterial species sourced from hot springs) display stability across a wide range of temperatures, expanding the scope for scaffold selection. This chapter will cover some of the common methods of protein functionalization as well as some specific examples of popular functionalization methods reported in the literature. It will then present three case studies showing examples of how functionalization and imaging of proteins and protein-based structures can be achieved.",
keywords = "Biosensor, Conjugation, Crosslinking, Functionalization, Gold nanoparticles, Nanofibril, Peroxiredoxin, Quantum dot, Scaffold, Surface",
author = "Kyle Webster and Luigi Sasso and Domigan, {Laura J.}",
year = "2020",
doi = "10.1007/978-1-4939-9869-2_8",
language = "English",
isbn = "978-1-4939-9868-5",
series = "Methods in Molecular Biology",
publisher = "Springer",
pages = "119--147",
editor = "Gerrard, {Juliet A.} and Domigan, {Laura J.}",
booktitle = "Protein Nanotechnology",

}

RIS

TY - CHAP

T1 - Adding Function to Protein Scaffolds

AU - Webster, Kyle

AU - Sasso, Luigi

AU - Domigan, Laura J.

PY - 2020

Y1 - 2020

N2 - Biological systems often outperform artificial ones in ordering, assembly, and diversity of structure at the nanoscale. Proteins are particularly remarkable in this context. Through oligomerization, protein monomers assemble on multiple length scales, into larger and more complex structures such as viral capsids, filaments, and regulatory complexes. It is this structural diversity that makes proteins attractive candidates for use as functionalizable scaffolds. Well-established protein structure databases such as the protein data bank (PDB) allow researchers to search for a structure that fits their requirements, allowing them access to shapes and assembly mechanisms that would otherwise be difficult to achieve. Then, by employing functionalization techniques to conjugate artificial or biological molecules to their protein scaffold of choice, researchers can access chemistries beyond the limits of the 20 commonly occurring natural amino acids. Additionally, proteins, with a few exceptions, operate at physiological pH and temperature, making them ideal for medical applications and/or low-cost manufacture. Additionally, proteins sourced from extremophiles such as Thermus aquaticus (a bacterial species sourced from hot springs) display stability across a wide range of temperatures, expanding the scope for scaffold selection. This chapter will cover some of the common methods of protein functionalization as well as some specific examples of popular functionalization methods reported in the literature. It will then present three case studies showing examples of how functionalization and imaging of proteins and protein-based structures can be achieved.

AB - Biological systems often outperform artificial ones in ordering, assembly, and diversity of structure at the nanoscale. Proteins are particularly remarkable in this context. Through oligomerization, protein monomers assemble on multiple length scales, into larger and more complex structures such as viral capsids, filaments, and regulatory complexes. It is this structural diversity that makes proteins attractive candidates for use as functionalizable scaffolds. Well-established protein structure databases such as the protein data bank (PDB) allow researchers to search for a structure that fits their requirements, allowing them access to shapes and assembly mechanisms that would otherwise be difficult to achieve. Then, by employing functionalization techniques to conjugate artificial or biological molecules to their protein scaffold of choice, researchers can access chemistries beyond the limits of the 20 commonly occurring natural amino acids. Additionally, proteins, with a few exceptions, operate at physiological pH and temperature, making them ideal for medical applications and/or low-cost manufacture. Additionally, proteins sourced from extremophiles such as Thermus aquaticus (a bacterial species sourced from hot springs) display stability across a wide range of temperatures, expanding the scope for scaffold selection. This chapter will cover some of the common methods of protein functionalization as well as some specific examples of popular functionalization methods reported in the literature. It will then present three case studies showing examples of how functionalization and imaging of proteins and protein-based structures can be achieved.

KW - Biosensor

KW - Conjugation

KW - Crosslinking

KW - Functionalization

KW - Gold nanoparticles

KW - Nanofibril

KW - Peroxiredoxin

KW - Quantum dot

KW - Scaffold

KW - Surface

UR - http://www.scopus.com/inward/record.url?scp=85073179577&partnerID=8YFLogxK

U2 - 10.1007/978-1-4939-9869-2_8

DO - 10.1007/978-1-4939-9869-2_8

M3 - Chapter

SN - 978-1-4939-9868-5

T3 - Methods in Molecular Biology

SP - 119

EP - 147

BT - Protein Nanotechnology

A2 - Gerrard, Juliet A.

A2 - Domigan, Laura J.

PB - Springer

CY - New York, NY, USA

ER -

ID: 68570086