Distinct Molten-globule Conformations in an Interacting Protein Domain Resolved via 19F NMR of Fluoroprolines

The files NCBD_WT.zip, NCBD_P13S.zip, NCBD_P13R.zip, NCBD_P30S.zip and NCBD_P30R.zip contains both NMR data and structural models of five variants of a small protein, NCBD with either natural amino-acids (WT) or a 4R fluoroproline either at position 13 and 30 (P13R or P30R) or a 4S fluoroproline either at position 13 and 30 (P13S or P30S). The archive contains two folders named "data" (containing the NMR peak lists used for the structure calculation) and "refine" that contains the output of the ARIA 2.2 program.

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Publication Details

Journal
Zenodo (CERN European Organization for Nuclear Research)
Published
2025-11-27
DOI
https://doi.org/10.5281/zenodo.17739276
Primary Topic
Protein Structure and Dynamics
Type
article
Field-Weighted Citation Impact
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article

Distinct Molten-globule Conformations in an Interacting Protein Domain Resolved via 19F NMR of Fluoroprolines

Zenodo (CERN European Organization for Nuclear Research)
Protein Structure and Dynamics
article

Distinct Molten-globule Conformations in an Interacting Protein Domain Resolved via 19F NMR of Fluoroprolines

article en

Abstract

The files NCBD_WT.zip, NCBD_P13S.zip, NCBD_P13R.zip, NCBD_P30S.zip and NCBD_P30R.zip contains both NMR data and structural models of five variants of a small protein, NCBD with either natural amino-acids (WT) or a 4R fluoroproline either at position 13 and 30 (P13R or P30R) or a 4S fluoroproline either at position 13 and 30 (P13S or P30S). The archive contains two folders named "data" (containing the NMR peak lists used for the structure calculation) and "refine" that contains the output of the ARIA 2.2 program.

Zenodo (CERN European Organization for Nuclear Research)
Université de Strasbourg (FR)
Openalex Percentile: Top 42%
Protein Structure and Dynamics
DOIOpen Access PDFOpenAlex
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Distinct Molten-globule Conformations in an Interacting Protein Domain Resolved via 19F NMR of Fluoroprolines · Zenodo (CERN European Organization for Nuclear Research) (2025) | TGRS Research Map | TGRS