scholarly journals Conformational characterization of the intrinsically disordered protein Chibby: Interplay between structural elements in target recognition

2016 ◽  
Vol 25 (8) ◽  
pp. 1420-1429 ◽  
Author(s):  
Ryan C. Killoran ◽  
Modupeola A. Sowole ◽  
Mohammad A. Halim ◽  
Lars Konermann ◽  
Wing-Yiu Choy
Keyword(s):  
Target Recognition ◽  
Intrinsically Disordered Protein ◽  
Structural Elements ◽  
Intrinsically Disordered ◽  
Disordered Protein

scholarly journals Folding and Characterization of Intrinsically Disordered Protein Human Cyclin I (Ccni)

2012 ◽  
Vol 102 (3) ◽  
pp. 634a-635a
Author(s):  
Hsueh-Liang Chu ◽  
Tsai-Mu Cheng ◽  
Hsing-Yuan Li ◽  
Chia-Ching Chang
Keyword(s):  
Intrinsically Disordered Protein ◽  
Intrinsically Disordered ◽  
Disordered Protein ◽  
Cyclin I

Structural and Kinetic Characterization of the Intrinsically Disordered Protein SeV NTAIL through Enhanced Sampling Simulations

2017 ◽  
Vol 121 (41) ◽  
pp. 9572-9582 ◽  
Author(s):  
Mattia Bernetti ◽  
Matteo Masetti ◽  
Fabio Pietrucci ◽  
Martin Blackledge ◽  
Malene Ringkjobing Jensen ◽  
...  
Keyword(s):  
Intrinsically Disordered Protein ◽  
Kinetic Characterization ◽  
Enhanced Sampling ◽  
Intrinsically Disordered ◽  
Disordered Protein

scholarly journals High-resolution structural characterization of Noxa, an intrinsically disordered protein, by microsecond molecular dynamics simulations

2015 ◽  
Vol 11 (7) ◽  
pp. 1850-1856 ◽  
Author(s):  
L. Michel Espinoza-Fonseca ◽  
Ameeta Kelekar
Keyword(s):  
Molecular Dynamics ◽  
High Resolution ◽  
Molecular Dynamics Simulations ◽  
Intrinsically Disordered Protein ◽  
Atomic Level ◽  
Intrinsically Disordered ◽  
Disordered Protein ◽  
Functional Features ◽  
Dynamics Simulations

Microsecond molecular dynamics simulations reveal structural and functional features of Noxa, an intrinsically disordered protein, at atomic-level resolution.

Monitoring structural changes in intrinsically disordered proteins using QCM-D: application to the bacterial cell division protein ZipA

2016 ◽  
Vol 52 (39) ◽  
pp. 6541-6544 ◽  
Author(s):  
Pablo Mateos-Gil ◽  
Achilleas Tsortos ◽  
Marisela Vélez ◽  
Electra Gizeli
Keyword(s):  
Cell Division ◽  
Structural Changes ◽  
Intrinsically Disordered Proteins ◽  
Intrinsically Disordered Protein ◽  
Disordered Proteins ◽  
Bacterial Cell Division ◽  
Intrinsically Disordered ◽  
Disordered Protein ◽  
Cell Division Protein

Characterization of structural changes in an intrinsically disordered protein attached on a QCM-D, with a sensitivity of 1.8 nm or better.

scholarly journals Characterization of AMBN I and II Isoforms and Study of Their Ca2+-Binding Properties

2020 ◽  
Vol 21 (23) ◽  
pp. 9293
Author(s):  
Veronika Vetyskova ◽  
Monika Zouharova ◽  
Lucie Bednarova ◽  
Ondřej Vaněk ◽  
Petra Sázelová ◽  
...  
Keyword(s):  
Intrinsically Disordered Protein ◽  
Significant Feature ◽  
Amino Acid Residues ◽  
Binding Properties ◽  
Specific Sequence ◽  
Intrinsically Disordered ◽  
Disordered Protein

Ameloblastin (Ambn) as an intrinsically disordered protein (IDP) stands for an important role in the formation of enamel—the hardest biomineralized tissue commonly formed in vertebrates. The human ameloblastin (AMBN) is expressed in two isoforms: full-length isoform I (AMBN ISO I) and isoform II (AMBN ISO II), which is about 15 amino acid residues shorter than AMBN ISO I. The significant feature of AMBN—its oligomerization ability—is enabled due to a specific sequence encoded by exon 5 present at the N-terminal part in both known isoforms. In this study, we characterized AMBN ISO I and AMBN ISO II by biochemical and biophysical methods to determine their common features and differences. We confirmed that both AMBN ISO I and AMBN ISO II form oligomers in in vitro conditions. Due to an important role of AMBN in biomineralization, we further addressed the calcium (Ca2+)-binding properties of AMBN ISO I and ISO II. The binding properties of AMBN to Ca2+ may explain the role of AMBN in biomineralization and more generally in Ca2+ homeostasis processes.

scholarly journals The MemMoRF database for recognizing disordered protein regions interacting with cellular membranes

2020 ◽  
Vol 49 (D1) ◽  
pp. D355-D360 ◽  
Author(s):  
Georgina Csizmadia ◽  
Gábor Erdős ◽  
Hedvig Tordai ◽  
Rita Padányi ◽  
Silvio Tosatto ◽  
...  
Keyword(s):  
Lipid Membrane ◽  
Chemical Shifts ◽  
Intrinsically Disordered Protein ◽  
Structural Data ◽  
Membrane Lipid ◽  
Order Transition ◽  
Intrinsically Disordered ◽  
Disordered Protein ◽  
Associated Proteins

Abstract Protein and lipid membrane interactions play fundamental roles in a large number of cellular processes (e.g. signalling, vesicle trafficking, or viral invasion). A growing number of examples indicate that such interactions can also rely on intrinsically disordered protein regions (IDRs), which can form specific reversible interactions not only with proteins but also with lipids. We named IDRs involved in such membrane lipid-induced disorder-to-order transition as MemMoRFs, in an analogy to IDRs exhibiting disorder-to-order transition upon interaction with protein partners termed Molecular Recognition Features (MoRFs). Currently, both the experimental detection and computational characterization of MemMoRFs are challenging, and information about these regions are scattered in the literature. To facilitate the related investigations we generated a comprehensive database of experimentally validated MemMoRFs based on manual curation of literature and structural data. To characterize the dynamics of MemMoRFs, secondary structure propensity and flexibility calculated from nuclear magnetic resonance chemical shifts were incorporated into the database. These data were supplemented by inclusion of sentences from papers, functional data and disease-related information. The MemMoRF database can be accessed via a user-friendly interface at https://memmorf.hegelab.org, potentially providing a central resource for the characterization of disordered regions in transmembrane and membrane-associated proteins.

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