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Jure Praznikar

dblp:281/5874 · DBLP profile ↗
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1ranked-venue papers
1as first author
1since 2021 · last 2026
0000-0003-1842-5181ORCID · reported

Domains — the database's venue-derived domains; a paper can count in several

Applied, interdisciplinary, general and emerging computing · 1 · 1 first-author · 1 since 2021

Expertise — from the expertise taxonomy: the topics of the expert's papers under the CCF categories. A weight counts papers with recency: 1 for a paper about the topic, 0.3 when the topic is its context, halved every five years.

Interdisciplinary, comprehensive, and emerging computing
1 paper
Bioinformatics and computational biology · 100%

Topics — the 2 heaviest of 2, each with the papers that count most for it

TopicWeightPapersLastEvidence papers
Bioinformatics and computational biology › protein structure analysis › protein flexibility
protein flexibility prediction
1.012026
Fast prediction of protein flexibility · Bioinform. 2026
Bioinformatics and computational biology
protein structure analysis
1.012026
Fast prediction of protein flexibility · Bioinform. 2026

Methods — techniques the papers use, named apart from their topics

molecular dynamics simulation · 1.0linear regression · 1.0graphlet degree vector · 1.0
YearPublicationVenuePosition
2026 Fast prediction of protein flexibility
abstract
MOTIVATION: Advances in hardware have made molecular dynamics (MD) simulations of protein structures faster and more accessible to the scientific community. However, accurately estimating protein flexibility using MD remains computationally demanding, especially for large systems and long time scales. Several MD-based resources-including MdMD, the DynamD database, and more recently ATLAS and mdCATH-now provide MD trajectories for thousands of proteins, enabling the development of predictive models. RESULTS: Here, the Graphlet Degree Vector (GDV) is introduced as a lightweight, fast, and easy-to-implement linear model for predicting protein flexibility directly from atom coordinates. GDV is a 15-dimensional feature vector that captures local packing and the spatial connectivity of each atom with its nearby neighbors. Trained on a subset of globular-like proteins from the ATLAS database, the GDV model achieves a Spearman correlation of 0.828 compared to MD data. The model trained on ATLAS dataset was further evaluated on independent Nuclear Magnetic Resonance and cryo-electron microscopy datasets, demonstrating the robustness and generalizability of the GDV-based approach. A key advantage of the GDV model is that it requires no additional external or experimental data and can be applied in near real time (on the order of 10 seconds) even for large proteins with 20 000 atoms on a standard desktop or laptop. Overall, the results show that a lightweight, fast, and purely coordinate-based model can provide accurate and generalizable predictions of protein flexibility across diverse folds and sizes. AVAILABILITY: The source code is available in the GitHub repository https://github.com/jure-praznikar/FastProtFlex. The data required for model training are available at https://doi.org/10.5281/zenodo.17771418. CONTACT: [email protected].
Jure Praznikar
Bioinform.1