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Homepage>BS Standards>07 MATHEMATICS. NATURAL SCIENCES>07.120 Nanotechnologies>PD ISO/TS 23459:2021 Nanotechnologies. Assessment of protein secondary structure during an interaction with nanomaterials using ultraviolet circular dichroism
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PD ISO/TS 23459:2021 Nanotechnologies. Assessment of protein secondary structure during an interaction with nanomaterials using ultraviolet circular dichroism

PD ISO/TS 23459:2021

Nanotechnologies. Assessment of protein secondary structure during an interaction with nanomaterials using ultraviolet circular dichroism

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Standard number:PD ISO/TS 23459:2021
Pages:36
Released:2021-02-10
ISBN:978 0 539 01802 8
Status:Standard
PD ISO/TS 23459:2021 - Nanotechnologies Standard

PD ISO/TS 23459:2021 - Nanotechnologies: Assessment of Protein Secondary Structure

Delve into the cutting-edge world of nanotechnology with the PD ISO/TS 23459:2021 standard. This comprehensive document is an essential resource for professionals and researchers who are involved in the study and application of nanomaterials, particularly in the context of their interaction with proteins. Released on February 10, 2021, this standard provides a detailed framework for assessing protein secondary structure using ultraviolet circular dichroism (UV CD), a powerful technique that offers insights into the conformational changes proteins undergo when interacting with nanomaterials.

Key Features of the Standard

  • Standard Number: PD ISO/TS 23459:2021
  • Pages: 36
  • Release Date: February 10, 2021
  • ISBN: 978 0 539 01802 8
  • Status: Standard

Understanding the Importance of Protein-Nanomaterial Interactions

Proteins are fundamental to biological processes, and their interactions with nanomaterials can significantly influence the behavior and efficacy of nanotechnology applications. The secondary structure of proteins, which includes alpha helices and beta sheets, is crucial for their function. Alterations in this structure can lead to changes in protein activity, stability, and interaction with other biomolecules.

The PD ISO/TS 23459:2021 standard provides a systematic approach to evaluating these structural changes, ensuring that researchers and developers can accurately assess the impact of nanomaterials on protein conformation. This is particularly important in fields such as drug delivery, biosensing, and the development of nanomedicines, where the interaction between proteins and nanomaterials can determine the success of a technology.

Ultraviolet Circular Dichroism: A Powerful Analytical Tool

Ultraviolet circular dichroism (UV CD) is a spectroscopic technique that measures the differential absorption of left-handed and right-handed circularly polarized light by chiral molecules, such as proteins. This method is highly sensitive to the secondary structure of proteins, making it an invaluable tool for researchers studying protein-nanomaterial interactions.

The PD ISO/TS 23459:2021 standard outlines the procedures and best practices for using UV CD to assess protein secondary structure. By following this standard, researchers can ensure that their measurements are accurate, reproducible, and comparable across different studies. This consistency is crucial for advancing our understanding of how nanomaterials interact with biological systems and for developing safe and effective nanotechnology applications.

Applications and Benefits

The insights gained from using the PD ISO/TS 23459:2021 standard can be applied across a wide range of industries and research areas. Some of the key applications and benefits include:

  • Drug Development: Understanding how nanomaterials interact with proteins can aid in the design of more effective drug delivery systems, ensuring that therapeutic agents reach their target sites without being prematurely degraded or inactivated.
  • Biotechnology: The standard can help in the development of biosensors and diagnostic tools that rely on protein-nanomaterial interactions, leading to more sensitive and specific detection methods.
  • Environmental Science: Assessing the impact of nanomaterials on proteins in the environment can inform risk assessments and guide the development of safer nanotechnology products.
  • Material Science: Insights into protein-nanomaterial interactions can drive the innovation of new materials with tailored properties for specific applications.

Why Choose PD ISO/TS 23459:2021?

Choosing the PD ISO/TS 23459:2021 standard means investing in a reliable and authoritative resource that is recognized globally. This standard is developed by experts in the field of nanotechnology and protein chemistry, ensuring that it reflects the latest scientific knowledge and technological advancements.

By adhering to this standard, organizations can demonstrate their commitment to quality and safety, enhancing their reputation and credibility in the industry. Moreover, the standard provides a common language and framework for collaboration, facilitating partnerships and knowledge exchange between researchers, developers, and regulatory bodies.

Conclusion

The PD ISO/TS 23459:2021 standard is an indispensable tool for anyone involved in the study or application of nanotechnologies. By providing a clear and detailed methodology for assessing protein secondary structure during interactions with nanomaterials, this standard supports the development of innovative and safe nanotechnology solutions. Whether you are a researcher, developer, or industry professional, the insights and guidance offered by this standard will be invaluable in advancing your work and achieving your goals.

DESCRIPTION

PD ISO/TS 23459:2021


This standard PD ISO/TS 23459:2021 Nanotechnologies. Assessment of protein secondary structure during an interaction with nanomaterials using ultraviolet circular dichroism is classified in these ICS categories:
  • 07.120 Nanotechnologies

This document specifies measurement protocols and test conditions to determine alterations to protein secondary structure induced by their interaction with nanomaterials using ultraviolet circular dichroism (UV-CD) spectroscopy.

This document does not apply to the characterization of conformational changes of disordered proteins.