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Protein B-factor, also known as the Debye-Waller temperature factor or atomic displacement parameter, measures the thermal fluctuation of an atom around its average position. It serves as a crucial indicator of protein flexibility and dynamics. However, accurately predicting the B-factor of Cα atoms remains challenging. In this work, we introduce OPUS-BFactor, a tool for predicting the normalized protein B-factor. OPUS-BFactor employs a transformer-based module to integrate sequence-level and pair-level features, encompassing structural attributes derived from the protein's 3D structure and evolutionary profiles obtained from the protein language model ESM-2. Specifically, OPUS-BFactor treats pair features as a bias term, incorporating them into the attention matrix derived from the sequence-level features of each residue pair, thereby effectively merging pair features with sequence features. OPUS-BFactor operates in two modes, enabling predictions based solely on either the protein sequence or the 3D structure of the target protein. Evaluation on three test sets, including recently released targets from CAMEO and CASP15, demonstrated that OPUS-BFactor significantly outperformed other B-factor prediction methods. Therefore, OPUS-BFactor is a valuable tool for predicting protein properties related to the B-factor, such as flexibility, thermal stability, and regional activity.
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http://dx.doi.org/10.3390/molecules30122570 | DOI Listing |
ACS Omega
September 2025
Laboratório de Biotecnologia Farmacêutica (pbiotech), Faculdade de Farmácia, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ 21941-902, Brazil.
The crystallographic B-factor (Bf), also known as the Debye-Waller factor (DWF) or temperature factor, relates to the mean-square displacement of the atoms (X). X may be composed of individual contributions from lattice disorder (LT), static conformational heterogeneity (H) throughout the lattice, rigid body vibration (RB), local conformational vibration (V), and zero-point atomic fluctuation (A). The Bf has been widely employed as a surrogate measure of local protein flexibility, although such relation has not been confirmed.
View Article and Find Full Text PDFFront Immunol
August 2025
Shenzhen Hospital, Southern Medical University, Shenzhen, China.
Transplant-associated thrombotic microangiopathy (TA-TMA) is a severe complication of hematopoietic stem cell transplantation (HSCT), characterized by microangiopathic hemolytic anemia, thrombocytopenia, microthrombosis, and multi-organ dysfunction. Mortality rates range from 50% to 90%, with higher rates observed in high-risk patients. The pathogenesis of TA-TMA involves abnormal activation of the complement system-particularly of the alternative pathway-resulting in endothelial injury and microthrombosis.
View Article and Find Full Text PDFIEEE Trans Comput Biol Bioinform
January 2025
B-factor is a measure of ray attenuation or scattering caused by atomic thermal motion during X-ray diffraction of protein crystal structure. B-factor reflects the vibration of atoms; hence, it is the most common experimental descriptor of protein flexibility and has been extensively applied in the studies of protein dynamics, screening of bioactive small molecules, and protein engineering. The prediction of B-factor profiles has considerable significance for analyzing the dynamic properties of unknown proteins.
View Article and Find Full Text PDFPak J Pharm Sci
August 2025
Department of Horticulture and Life Science, Yeungnam University, Republic of Korea.
This study aims to investigate the therapeutic properties of Eichhornia crassipes (Mart.) Solms, demonstrating its sedative and muscle relaxant capabilities. It examines molecular dynamics simulations, docking investigations, in silico screening and molecular interactions.
View Article and Find Full Text PDFActa Crystallogr F Struct Biol Commun
August 2025
Department of Chemistry and Biochemistry, University of Arkansas at Fayetteville, Fayetteville, AR 72701, USA.
Here, we report the crystal structure of Escherichia coli glucokinase (GLK), which has phosphate bound in the cleft between the α and β domains adjacent to the active site. A ternary complex consisting of GLK, glucose and phosphate is also reported in this work. Diffraction data were collected at 2.
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