The Role of Rotational Motion in Diffusion NMR Experiments on Supramolecular Assemblies: Application to Sup35NM Fibrils

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The Role of Rotational Motion in Diffusion NMR Experiments on Supramolecular Assemblies: Application to Sup35NM Fibrils. / Kharkov, Boris B. ; Podkorytov, Ivan S. ; Bondarev, Stanislav A. ; Belousov, Mikhail V. ; Salikov, Vladislav A. ; Zhouravleva, Galina A. ; Skrynnikov, Nikolai R. .

In: ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, Vol. 60, No. 28, 05.07.2021, p. 15445-15451.

Research output: Contribution to journal › Article › peer-review

BibTeX

@article{7eda0867c12748e59f19413d8fc21a84,

title = "The Role of Rotational Motion in Diffusion NMR Experiments on Supramolecular Assemblies: Application to Sup35NM Fibrils",

abstract = "Pulsed-field gradient (PFG) NMR is an important tool for characterization of biomolecules and supramolecular assemblies. However, for micrometer-sized objects, such as amyloid fibrils, these experiments become difficult to interpret because in addition to translational diffusion they are also sensitive to rotational diffusion. We have constructed a mathematical theory describing the outcome of PFG NMR experiments on rod-like fibrils. To test its validity, we have studied the fibrils formed by Sup35NM segment of the prion protein Sup35. The interpretation of the PFG NMR data in this system is fully consistent with the evidence from electron microscopy. Contrary to some previously expressed views, the signals originating from disordered regions in the fibrils can be readily differentiated from the similar signals representing small soluble species (e.g. proteolytic fragments). This paves the way for diffusion-sorted NMR experiments on complex amyloidogenic samples.",

keywords = "amyloid fibrils, NMR spectroscopy, proteins, pulsed-field gradient diffusion measurements, Sup35, PROTEIN, GREEN-FUNCTION FORMULATION, DETERMINANT, PRION, TRANSLATION, AMYLOID FIBRILS, ROD-LIKE POLYMERS, DYNAMICS, TERMINATION, AGGREGATION",

author = "Kharkov, {Boris B.} and Podkorytov, {Ivan S.} and Bondarev, {Stanislav A.} and Belousov, {Mikhail V.} and Salikov, {Vladislav A.} and Zhouravleva, {Galina A.} and Skrynnikov, {Nikolai R.}",

note = "Publisher Copyright: {\textcopyright} 2021 Wiley-VCH GmbH",

year = "2021",

month = jul,

day = "5",

doi = "10.1002/anie.202102408",

language = "English",

volume = "60",

pages = "15445--15451",

journal = "ANGEWANDTE CHEMIE-INTERNATIONAL EDITION",

issn = "1433-7851",

publisher = "Wiley-Blackwell",

number = "28",

}

RIS

TY - JOUR

T1 - The Role of Rotational Motion in Diffusion NMR Experiments on Supramolecular Assemblies: Application to Sup35NM Fibrils

AU - Kharkov, Boris B.

AU - Podkorytov, Ivan S.

AU - Bondarev, Stanislav A.

AU - Belousov, Mikhail V.

AU - Salikov, Vladislav A.

AU - Zhouravleva, Galina A.

AU - Skrynnikov, Nikolai R.

PY - 2021/7/5

Y1 - 2021/7/5

N2 - Pulsed-field gradient (PFG) NMR is an important tool for characterization of biomolecules and supramolecular assemblies. However, for micrometer-sized objects, such as amyloid fibrils, these experiments become difficult to interpret because in addition to translational diffusion they are also sensitive to rotational diffusion. We have constructed a mathematical theory describing the outcome of PFG NMR experiments on rod-like fibrils. To test its validity, we have studied the fibrils formed by Sup35NM segment of the prion protein Sup35. The interpretation of the PFG NMR data in this system is fully consistent with the evidence from electron microscopy. Contrary to some previously expressed views, the signals originating from disordered regions in the fibrils can be readily differentiated from the similar signals representing small soluble species (e.g. proteolytic fragments). This paves the way for diffusion-sorted NMR experiments on complex amyloidogenic samples.

AB - Pulsed-field gradient (PFG) NMR is an important tool for characterization of biomolecules and supramolecular assemblies. However, for micrometer-sized objects, such as amyloid fibrils, these experiments become difficult to interpret because in addition to translational diffusion they are also sensitive to rotational diffusion. We have constructed a mathematical theory describing the outcome of PFG NMR experiments on rod-like fibrils. To test its validity, we have studied the fibrils formed by Sup35NM segment of the prion protein Sup35. The interpretation of the PFG NMR data in this system is fully consistent with the evidence from electron microscopy. Contrary to some previously expressed views, the signals originating from disordered regions in the fibrils can be readily differentiated from the similar signals representing small soluble species (e.g. proteolytic fragments). This paves the way for diffusion-sorted NMR experiments on complex amyloidogenic samples.

KW - amyloid fibrils

KW - NMR spectroscopy

KW - proteins

KW - pulsed-field gradient diffusion measurements

KW - Sup35

KW - PROTEIN

KW - GREEN-FUNCTION FORMULATION

KW - DETERMINANT

KW - PRION

KW - TRANSLATION

KW - AMYLOID FIBRILS

KW - ROD-LIKE POLYMERS

KW - DYNAMICS

KW - TERMINATION

KW - AGGREGATION

UR - http://www.scopus.com/inward/record.url?scp=85107162206&partnerID=8YFLogxK

UR - https://www.mendeley.com/catalogue/5d7648b0-7381-3a68-b9d8-0bfab6cdbd63/

U2 - 10.1002/anie.202102408

DO - 10.1002/anie.202102408

M3 - Article

VL - 60

SP - 15445

EP - 15451

JO - ANGEWANDTE CHEMIE-INTERNATIONAL EDITION

JF - ANGEWANDTE CHEMIE-INTERNATIONAL EDITION

SN - 1433-7851

IS - 28

ER -

ID: 77759931