Protein activity regulation by conformational entropy

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Conformational entropy in molecular recognition by proteins

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Dynamically driven protein allostery

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Protein dynamics from NMR.

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Detecting the Undetectable: Functional Protein Motions in the Hidden Timescale Window Revealed by NMR Relaxation Measurements

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Evaluation of the Influence of Biosurface Design on the Interaction between the Regulatory Peptide RS1‐reg and ODC1 Reveals a Membrane‐Dependent Affinity Increase

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Structure- and Dynamics-guided Drug Development Using NMR and its Application to Diverse Pharmaceutical Modalities

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Study of reactive dye/serum albumin interactions: thermodynamic parameters, protein alterations and computational analysis

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Heterogeneity in the M. tuberculosis β-lactamase inhibition by SulbactamPreprint

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Principles Governing Molecular Recognition

Demchenko, A. P. (2023) · Springer eBooks · doi:10.1007/978-3-031-19089-6_1

Decoding the Dual Recognition Mechanism of Glucocorticoid Receptor for DNA and RNA: Sequence vs. ShapePreprint

Hörberg, J., & Reymer, A. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.03.15.532803

Double and triple thermodynamic mutant cycles reveal the basis for specific MsbA-lipid interactionsPreprint

Lyu, J., Zhang, T., Marty, M. T., Clemmer, D. E., Russell, D. H., & Laganowsky, A. D. (2023) · eLife · doi:10.7554/elife.91094.1

Reviewer #2 (Public Review): A parametrized two-domain thermodynamic model explains diverse mutational effects on protein allostery

(2023) · eLife · doi:10.7554/elife.92262.1.sa1

Reviewer #3 (Public Review): A parametrized two-domain thermodynamic model explains diverse mutational effects on protein allostery

(2023) · eLife · doi:10.7554/elife.92262.1.sa0

Reviewer #1 (Public Review): A parametrized two-domain thermodynamic model explains diverse mutational effects on protein allostery

(2023) · eLife · doi:10.7554/elife.92262.1.sa2

Investigating Quantum Coherence of N-Methylpyrrole Through Vibrational Spectroscopy and Potential Energy: Theoretical StudyPreprint

An, H., Qin, C., Abulimiti, B., Xiang, M., & Wang, X. (2024) · SSRN Electronic Journal · doi:10.2139/ssrn.4799717

Cyclization of ubiquitin chains reinforces their recognition by ZNF 216

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Enhancing the biological insight from limited proteolysis-coupled mass spectrometryPreprint

Nagel, L., Großbach, J., Cappelletti, V., Dörig, C., Picotti, P., & Beyer, A. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.06.12.598633

Dynamic regions allosterically connect the USP14 active site with the proteasome interaction surfacePreprint

Salomonsson, J., Sjöstrand, L., Eskilson, A., Derbyshire, D. J., D’Arcy, P., Sunnerhagen, M., & Ahlner, A. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.06.28.601165

Entropy‐Driven Self‐Assembly of DNA Origami Isomers

Wu, H., Xu, X., Wei, B., & Lakerveld, R. (2024) · Small Structures · doi:10.1002/sstr.202400220

Positive activation entropy of Bacillus circulans xylanase catalyzed ONPX2 hydrolysis: A mechanistic and engineering study

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Modulating the Aggregation States of a Pd 6 L 4 Cage for Selectivity Flipping during the Stereo‐Divergent Semi‐Hydrogenation of Alkynes

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Structural basis of the π-stacking network governing cofactor-substrate cooperativity of SbSOMTPreprint

Pow, K. C., Zhang, N., Yan, M., Wang, X., Lui, A. C. W., Lo, C., & Hao, Q. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.22.683835

Advances in Quantum Mechanical Methods for the Computation of Protein-Ligand Binding Free Energy

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Understanding Protein–Protein Interactions in Biology: Applications of NMR Spectroscopy and Isothermal Titration Calorimetry

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DT-TRAP enables accurate target recognition via simplified dosing and low-temperature incubation

Zhang, H., Yuan, W., Li, Y., Li, C., Xie, Y., Wan, N., Hao, H., & Ye, H. (2026) · Journal of Pharmaceutical Analysis · doi:10.1016/j.jpha.2026.101605

Protein disorder controls allostery in DNAPreprint

Rosenblum, G., Terterov, I., Mishra, S. K., Elad, N., Gianga, T., Hussain, R., Siligardi, G., & Hofmann, H. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.03.17.710445

Structure-guided design and rapid cell-free screening of a superior restriction endonuclease DpnI mutant to enhance the specific activity and efficiency of site-directed mutagenesis

Zhang, D., Ren, H., Wang, Y., Jin, N., Feng, X., Liu, M., Luo, Z., & Lu, C. (2026) · Bioscience Biotechnology and Biochemistry · doi:10.1093/bbb/zbag038

ONEST: a web-based platform for the rapid and robust analysis of protein excited states through CEST spectroscopy

Choi, J., Lee, S.-Y., Han, K., Carneiro, M. G., Ryu, K., & Lee, D. (2026) · Bioinformatics · doi:10.1093/bioinformatics/btag158

Déterminants moléculaires de l'affinité de l'intéraction entre la protéine désordonnée NTAIL et son partenaire XD chez le virus de la rougeole

Dosnon, M. (2015) · theses.fr (ABES) · doi:10.70675/4b22b8f8za593z4eccza290zbc1af2c63f30

Etude des relations structurales et fonctionnelles entre le domaine 2 de la protéine NS5A du virus de l’hépatite C et la Cyclophiline A humaine

Dujardin, M. (2015) · theses.fr (ABES) · doi:10.70675/c69e4bebz6eb7z4a22zb1d5z6a6359ad722b

Les protéines de nucléocapside du VIH-1 : structures, dynamiques, propriétés de fixation et de déstabilisation des acides nucléiques

Belfetmi, A. (2017) · theses.fr (ABES) · doi:10.70675/2fa3c5d6z2db6z41b0z8d46z342ee7b65514

Dynamique structurale de complexes RCPG - neuropeptides

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Navigating the knotty paths: Structures, folding, and functions of topologically knotted proteins

Puri, S., & Hsu, S. D. (2026) · Elsevier eBooks · doi:10.1016/b978-0-323-99507-8.00077-9

Newton’s cradle-like allosteric mechanism explains regulatory RsmE RNA binding

Finol, E., Damberger, F. F., Krepl, M., Flügel, T., Dietrich, P., Michaels, T. C. T., Vögeli, B., Šponer, J., & Allain, F. H. ‐. (2026) · Nature Communications · doi:10.1038/s41467-026-72126-z

Binding Entropy Can Be Predicted by Crystallographic EnsemblesPreprint

Miller, C. A., & Wankowicz, S. A. M. (2026) · eLife · doi:10.7554/elife.111298.1

Binding Entropy Can Be Predicted by Crystallographic EnsemblesPreprint

Miller, C. A., & Wankowicz, S. A. M. (2026) · eLife · doi:10.7554/elife.111298

DNA‐Induced Entropic Gain Triggers an Allosteric Switch for Biomolecular Condensation of Heat Shock Transcription Factor 1

Kawagoe, S., Kumeta, H., & Saio, T. (2026) · Angewandte Chemie · doi:10.1002/ange.7340537

DNA‐Induced Entropic Gain Triggers an Allosteric Switch for Biomolecular Condensation of Heat Shock Transcription Factor 1

Kawagoe, S., Kumeta, H., & Saio, T. (2026) · Angewandte Chemie International Edition · doi:10.1002/anie.7340537

Structural basis for substrate recognition by the pain-associated neuronal polyamine transporter SLC45A4

Sarode, V. V., Dutta, S., Singh, M. K., Pati, S., & Dehury, B. (2026) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2026.153275

Sidechain Dynamics and Allosteric Signaling in a PDZ Domain

Kornev, A. P. (2026) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.6c01858

Conformational entropy in complex molecular systems: computational strategies, machine learning, and emerging applications

Zhai, Y., Chen, Y.-X., Luo, J.-J., Ma, M.-Y., & Liu, F. (2026) · Chemické zvesti · doi:10.1007/s11696-026-05445-6

Dynamic view of an allosteric intermediate in a positively cooperative dimerPreprint

Sapienza, P. J., Mileur, T. R., Khan, M. S., Li, K., Aubé, J., & Lee, A. L. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.08.11.744235

Beyond structures: solution NMR as the quantitative engine of integrated structural biology

Purslow, J. A., & Venditti, V. (2026) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2026.1941622

AutoHMD: scalable and accurate validation of antibody–antigen complexes by heated molecular dynamics

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Native Ion Mobility–Mass Spectrometry Reports Kinetically Trapped Conformational Ensembles, Not Single Structures

Bleiholder, C., & Liu, F. C. (2026) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.6c00178

BindingDB Entry 50005685: Conformational restriction approach to β-secretase (BACE1) inhibitors III: effective investigation of the binding mode by combinational use of X-ray analysis, isothermal titration calorimetry and theoretical calculations.

BindingDB (2020) · UC San Diego · doi:10.7270/q25h7k6q

BindingDB Entry 50009378: Allosteric Modulator Discovery: From Serendipity to Structure-Based Design.

BindingDB (2021) · UC San Diego · doi:10.7270/q2c53q9m

RNA 3D Structure Analysis and Validation, and Design Algorithms for Proteins and RNA

Jain, S. (2015) · DukeSpace (Duke University)

Dynamic binding

Baldwin, A. J., & Kay, L. E. (2012) · Nature · doi:10.1038/488165a · Cited by 14

Entropy controls activity

Montoya, M. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2361

The dark energy of proteins comes to light: conformational entropy and its role in protein function revealed by NMR relaxation

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Dynamic activation of an allosteric regulatory protein

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Conformational entropy in molecular recognition by proteins

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