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Title: Unveiling the nanoscale architectures and dynamics of protein assembly with in situ atomic force microscopy

Journal Article · · Aggregate
DOI: https://doi.org/10.1002/agt2.604 · OSTI ID:2368966
ORCiD logo [1];  [2];  [3]; ORCiD logo [2];  [1]
  1. Laboratory of Soft Matter Physics, Institute of Physics Chinese Academy of Sciences Beijing China
  2. Physical Sciences Division Pacific Northwest National Laboratory Richland Washington USA, Department of Materials Science and Engineering University of Washington Seattle Washington USA
  3. Department of Materials Science and Engineering University of Washington Seattle Washington USA

Abstract Proteins play a vital role in different biological processes by forming complexes through precise folding with exclusive inter‐ and intra‐molecular interactions. Understanding the structural and regulatory mechanisms underlying protein complex formation provides insights into biophysical processes. Furthermore, the principle of protein assembly gives guidelines for new biomimetic materials with potential applications in medicine, energy, and nanotechnology. Atomic force microscopy (AFM) is a powerful tool for investigating protein assembly and interactions across spatial scales (single molecules to cells) and temporal scales (milliseconds to days). It has significantly contributed to understanding nanoscale architectures, inter‐ and intra‐molecular interactions, and regulatory elements that determine protein structures, assemblies, and functions. This review describes recent advancements in elucidating protein assemblies with in situ AFM. We discuss the structures, diffusions, interactions, and assembly dynamics of proteins captured by conventional and high‐speed AFM in near‐native environments and recent AFM developments in the multimodal high‐resolution imaging, bimodal imaging, live cell imaging, and machine‐learning‐enhanced data analysis. These approaches show the significance of broadening the horizons of AFM and enable unprecedented explorations of protein assembly for biomaterial design and biomedical research.

Sponsoring Organization:
USDOE
OSTI ID:
2368966
Alternate ID(s):
OSTI ID: 2560780
Journal Information:
Aggregate, Journal Name: Aggregate Journal Issue: 5 Vol. 5; ISSN 2692-4560
Publisher:
Wiley Blackwell (John Wiley & Sons)Copyright Statement
Country of Publication:
Country unknown/Code not available
Language:
English

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