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  Improved physical models enable the investigation of molecular recognition in intrinsically disordered proteins at atomistic rsolution.

Robustelli, P., Piana-Agostinetti, S., Ibanez de Opakua, A., Giordanetto, F., Campbell-Bezat, C. K., Becker, S., et al. (2019). Improved physical models enable the investigation of molecular recognition in intrinsically disordered proteins at atomistic rsolution. Biophysical Journal, 116(Suppl_1), 303A-303A. doi:10.1016/j.bpj.2018.11.1644.

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 Creators:
Robustelli, P., Author
Piana-Agostinetti, S., Author
Ibanez de Opakua, A.1, Author           
Giordanetto, F., Author
Campbell-Bezat, C. K., Author
Becker, S.2, Author           
Pan, A. C., Author
Zweckstetter, M.1, Author           
Shaw, D. E., Author
Affiliations:
1Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              
2Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

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Language(s): eng - English
 Dates: 2019-02-15
 Publication Status: Published online
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.bpj.2018.11.1644
 Degree: -

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Title: 63rd Annual Meeting of the Biophysical-Society
Place of Event: Baltimore, MD
Start-/End Date: 2019-03-02 - 2019-03-06

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Title: Biophysical Journal
Source Genre: Journal
 Creator(s):
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Publ. Info: 3
Pages: - Volume / Issue: 116 (Suppl_1) Sequence Number: - Start / End Page: 303A - 303A Identifier: -