Nature Biotechnology - John Gurdon 1933–2025

Smoking, infections and alcohol are the top causes

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Careers Across Academia and Industry

In the past two decades, lung cancer screening (LCS) with low-dose computed tomography (LDCT) has emerged as one of the most effective strategies for reducing lung cancer mortality. Landmark trials, i...

Careers Across Academia and Industry

Not 100% sure whether becoming *my* new colleague is a win or a threat, 😂 but the amazing PSDA group at AstraZeneca is looking for new faces to join a clever, fun, and interdisciplinary team! I believ...

UK science funding is currently facing a profound crisis, particularly for Life Sciences. Medical Research Council and BBSRC have paused researcher-led grant applications until the Spring, with no cle...

After careful consideration, Elsevier have made the difficult decision to sunset Researchfish on July 31st 2027, when the product will no longer be availab

Boards asked to recommend just three applications for funding, as BBSRC also suspends calls

Protein-ligand binding is governed by free energy, comprising both enthalpic and entropic contributions. Yet structural interpretations of binding thermodynamics have predominantly focused on enthalpic interactions, largely neglecting entropy because it is difficult to quantify from static structural models. Here, we developed multiconformer ensemble models to analyze high-resolution X-ray crystallography structures and estimate both protein and solvent conformational entropies. These ensemble models successfully predicted experimental binding entropies measured by isothermal titration calorimetry for over 70 protein-ligand pairs across 12 proteins, revealing a strong linear correlation. Protein entropy, estimated using crystallographic order parameters that capture both harmonic and anharmonic motion, correlates linearly with experimental binding entropy. Incorporating resolution-corrected differences in water-molecule counts substantially improves predictions, demonstrating that protein and solvent contributions must be considered jointly. Analysis of water-protein hydrogen bonding networks partially explains entropic differences across complexes. These results establish that crystallographic ensembles can quantify binding entropy, enabling explicit entropic considerations in structure-based studies of molecular recognition for both functional analysis and drug design. ### Competing Interest Statement The authors have declared no competing interest. American Cancer Society, https://ror.org/02e463172

How faddish ideas keep seducing.

Artificial intelligence boosts individual scientists’ output, citations and career progression, but collectively narrows research diversity and reduces collaboration, concentrating work in data-rich a...