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Predicting X‐ray solution scattering from flexible macromolecules

Published:2018-10-16 Issue:12 Volume:27 Page:2023-2036
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Zhou Hao¹,Guterres Hugo²,Mattos Carla²,Makowski Lee³

Affiliation:

1. Department of Electrical and Computer Engineering Northeastern University Boston Massachusetts

2. Department of Chemistry and Chemical Biology Northeastern University Boston Massachusetts

3. Department of Bioengineering Northeastern University Boston Massachusetts

Funder

NSF

National Institute of General Medical Sciences

National Institutes of Health

National Science Foundation

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/pro.3508

Reference47 articles.

1. Intrinsic motions along an enzymatic reaction trajectory

2. Three-dimensional triple-resonance NMR Spectroscopy of isotopically enriched proteins

3. Molecular Crowding Inhibits Intramolecular Breathing Motions in Proteins

4. X-ray solution scattering studies of the structural diversity intrinsic to protein ensembles

5. Modulation of HIV protease flexibility by the T80N mutation

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1. Integrating molecular dynamics simulation with small‐ and wide‐angle X‐ray scattering to unravel the flexibility, antigen‐blocking, and protease‐restoring functions in a hindrance‐based pro‐antibody;Protein Science;2024-08-15

2. SAXS/WAXS data of conformationally flexible ribose binding protein;Data in Brief;2024-02

3. Mechanisms of isoform-specific residue influence on GTP-bound HRas, KRas, and NRas;Biophysical Journal;2022-10

4. Isoform-Specific Destabilization of the Active Site Reveals Molecular Mechanism of Intrinsic Activation of KRas G13D;SSRN Electronic Journal;2019

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