Protein Folding upon Binding Revealed by Molecular Dynamics Simulation
Sign Up to like & getrecommendations! Published in 2017 at "Biophysical Journal"
DOI: 10.1016/j.bpj.2016.11.329
Abstract: Macromolecules frequently associate in living cells and tissues, where specific binding interactions based on dynamic conformation regulate molecular localization and activity. Despite the rapidly expanding experimental characterization of the structural proteome, the combinatorial explosion of… read more here.
Keywords: binding revealed; upon binding; folding upon; protein folding ... See more keywords
Hierarchical folding-upon-binding of an intrinsically disordered protein.
Sign Up to like & getrecommendations! Published in 2025 at "Nature communications"
DOI: 10.1038/s41467-025-66420-5
Abstract: Intrinsically disordered proteins (IDPs) often undergo folding-upon-binding to their partners via short linear motifs, typically 5-15 amino acids in length. However, a significant proportion of IDPs do not adhere to this paradigm but fold upon… read more here.
Keywords: folding upon; intrinsically disordered; disordered protein; folding intermediates ... See more keywords
Folding-upon-binding pathways of an intrinsically disordered protein from a deep Markov state model
Sign Up to like & getrecommendations! Published in 2024 at "Proceedings of the National Academy of Sciences of the United States of America"
DOI: 10.1073/pnas.2313360121
Abstract: Significance The biological functions of intrinsically disordered proteins are often mediated by sequence segments that fold into stable structures upon binding a structured partner protein. The molecular mechanisms by which disordered proteins recognize and bind… read more here.
Keywords: folding upon; intrinsically disordered; markov state; binding pathways ... See more keywords
Do antibody CDR loops change conformation upon binding?
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DOI: 10.1080/19420862.2024.2322533
Abstract: ABSTRACT Antibodies have increasingly been developed as drugs with over 100 now licensed in the US or EU. During development, it is often necessary to increase or reduce the affinity of an antibody and rational… read more here.
Keywords: change conformation; antibody; antigen; loops change ... See more keywords
Allosteric couplings upon binding of RfaH to transcription elongation complexes
Sign Up to like & getrecommendations! Published in 2022 at "Nucleic Acids Research"
DOI: 10.1093/nar/gkac453
Abstract: Abstract In every domain of life, NusG-like proteins bind to the elongating RNA polymerase (RNAP) to support processive RNA synthesis and to couple transcription to ongoing cellular processes. Structures of factor-bound transcription elongation complexes (TECs)… read more here.
Keywords: nusg rfah; transcription; transcription elongation; elongation complexes ... See more keywords
Structural rearrangements in mRNA upon its binding to human 80S ribosomes revealed by EPR spectroscopy
Sign Up to like & getrecommendations! Published in 2018 at "Nucleic Acids Research"
DOI: 10.1093/nar/gkx1136
Abstract: Abstract The model mRNA (MR), 11-mer RNA containing two nitroxide spin labels at the 5′- and 3′-terminal nucleotides and prone to form a stable homodimer (MR)2, was used for Electron Paramagnetic Resonance study of structural… read more here.
Keywords: rearrangements mrna; upon binding; structural rearrangements; binding human ... See more keywords
Accurate Prediction of Drug Activity by Computational Methods: Importance of Thermal Capacity
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DOI: 10.3390/molecules30122563
Abstract: Heat capacity is one of the most important thermodynamic quantities in protein biochemistry. Upon the binding of small molecules, a change in the heat capacity of proteins is generally observed, and this is often used… read more here.
Keywords: change heat; capacity; heat capacity; drug ... See more keywords