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Did you mean infolded protein binding (51 results)?
Ligand binding to a high-energy partially unfolded protein.
Kasper JR, Park C. Kasper JR, et al. Protein Sci. 2015 Jan;24(1):129-37. doi: 10.1002/pro.2596. Epub 2014 Dec 5. Protein Sci. 2015. PMID: 25367157 Free PMC article.
DHFR unfolds partially without releasing the ligand, though the binding affinity for NADP(+) is diminished upon partial unfolding. Based on known crystallographic structures of NADP(+) -bound DHFR and the model of the partially unfolded protein …
DHFR unfolds partially without releasing the ligand, though the binding affinity for NADP(+) is diminished upon partial unf …
The influence of intrinsic folding mechanism of an unfolded protein on the coupled folding-binding process during target recognition.
Xiong J, Gao M, Zhou J, Liu S, Su Z, Liu Z, Huang Y. Xiong J, et al. Proteins. 2019 Apr;87(4):265-275. doi: 10.1002/prot.25646. Epub 2018 Dec 27. Proteins. 2019. PMID: 30520528
Although the coupled folding-binding processes of IDPs have been extensively studied, it is still impossible to predict whether an unfolded protein is suitable for molecular signaling via coupled folding-binding. ...This accelerating effect is differen …
Although the coupled folding-binding processes of IDPs have been extensively studied, it is still impossible to predict whether an …
Thermodynamic analysis of a molecular chaperone binding to unfolded protein substrates.
Xu Y, Schmitt S, Tang L, Jakob U, Fitzgerald MC. Xu Y, et al. Biochemistry. 2010 Feb 16;49(6):1346-53. doi: 10.1021/bi902010t. Biochemistry. 2010. PMID: 20073505 Free PMC article.
Molecular chaperones are a highly diverse group of proteins that recognize and bind unfolded proteins to facilitate protein folding and prevent nonspecific protein aggregation. ...Thus, little is known about the relative binding affinities of different …
Molecular chaperones are a highly diverse group of proteins that recognize and bind unfolded proteins to facilitate protein fo …
Drug Binding to Partially Unfolded Serum Albumin: Insights into Nonsteroidal Anti-Inflammatory Drug Naproxen-BSA Interactions from Spectroscopic and MD Simulation Studies.
Rout D, Upadhyaya AK, Agarwala P, Sharma C, Pal A, Sasmal DK. Rout D, et al. J Phys Chem B. 2024 Oct 3;128(39):9327-9340. doi: 10.1021/acs.jpcb.4c03901. Epub 2024 Sep 24. J Phys Chem B. 2024. PMID: 39316707
Understanding the binding details of a small-molecule drug to a protein in its partially unfolded state is important for drug delivery as it provides insight into the overall drug-binding ability of the protein, even when the majority of bind …
Understanding the binding details of a small-molecule drug to a protein in its partially unfolded state is important fo …
Effects of Ligand Binding on the Energy Landscape of Acyl-CoA-Binding Protein.
Sonar P, Bellucci L, Mossa A, Heidarsson PO, Kragelund BB, Cecconi C. Sonar P, et al. Biophys J. 2020 Nov 3;119(9):1821-1832. doi: 10.1016/j.bpj.2020.09.016. Epub 2020 Sep 24. Biophys J. 2020. PMID: 33080224 Free PMC article.
Here, we use a combination of single-molecule optical tweezers and MD simulations to investigate the effect of ligand binding on the energy landscape of acyl-coenzyme A (CoA)-binding protein (ACBP). ACBP is a topologically simple and highly conserved four-alp …
Here, we use a combination of single-molecule optical tweezers and MD simulations to investigate the effect of ligand binding on the …
Effect of ligand binding on a protein with a complex folding landscape.
Mazal H , Aviram H , Riven I , Haran G . Mazal H , et al. Phys Chem Chem Phys. 2018 Jan 31;20(5):3054-3062. doi: 10.1039/c7cp03327c. Phys Chem Chem Phys. 2018. PMID: 28721412
Ligand binding to a protein can stabilize it significantly against unfolding. The variation of the folding free energy, deltadeltaG(0), due to ligand binding can be derived from a simple reaction scheme involving exclusive binding to the native …
Ligand binding to a protein can stabilize it significantly against unfolding. The variation of the folding free energy, …
Lessons about Protein Folding and Binding from Archetypal Folds.
Campos LA, Sadqi M, Muñoz V. Campos LA, et al. Acc Chem Res. 2020 Oct 20;53(10):2180-2188. doi: 10.1021/acs.accounts.0c00322. Epub 2020 Sep 11. Acc Chem Res. 2020. PMID: 32914959
In parallel, we and others set out to investigate the simplest possible protein structures capable of autonomous folding, which we defined as archetypal folds. The rationale was to recapitulate the hierarchical organization of protein structure, starting from the bo …
In parallel, we and others set out to investigate the simplest possible protein structures capable of autonomous folding, which we de …
Residual structures in the unfolded state of starch-binding domain of glucoamylase revealed by near-UV circular dichroism and protein engineering techniques.
Ota C, Ikeguchi M, Tanaka A, Hamada D. Ota C, et al. Biochim Biophys Acta. 2016 Oct;1864(10):1464-72. doi: 10.1016/j.bbapap.2016.05.002. Epub 2016 May 6. Biochim Biophys Acta. 2016. PMID: 27164491
Protein folding is a thermodynamic process driven by energy gaps between the native and unfolded states. Although a wealth of information is available on the structure of folded species, there is a paucity of data on unfolded species. Here, we analyzed the st …
Protein folding is a thermodynamic process driven by energy gaps between the native and unfolded states. Although a wealth of …
The Henipavirus V protein is a prevalently unfolded protein with a zinc-finger domain involved in binding to DDB1.
Salladini E, Delauzun V, Longhi S. Salladini E, et al. Mol Biosyst. 2017 Oct 24;13(11):2254-2267. doi: 10.1039/c7mb00488e. Mol Biosyst. 2017. PMID: 28972216
Henipavirus V proteins antagonize IFN signaling through PNT-mediated binding to STAT1, and several paramyxoviral V proteins promote STAT1 degradation through binding to DDB1. ...Using pull-down and MST we assessed their binding abilities towards DDB1. We show …
Henipavirus V proteins antagonize IFN signaling through PNT-mediated binding to STAT1, and several paramyxoviral V proteins promote S …
Decoding Structural Properties of a Partially Unfolded Protein Substrate: En Route to Chaperone Binding.
Nagpal S, Tiwari S, Mapa K, Thukral L. Nagpal S, et al. PLoS Comput Biol. 2015 Sep 22;11(9):e1004496. doi: 10.1371/journal.pcbi.1004496. eCollection 2015. PLoS Comput Biol. 2015. PMID: 26394388 Free PMC article.
The E.coli chaperone, GroEL binds with a large number of unfolded and partially folded proteins, to facilitate proper folding and prevent misfolding and aggregation. ...Further, we constructed network graphs to elucidate long-range intra-protein connectivity of nati …
The E.coli chaperone, GroEL binds with a large number of unfolded and partially folded proteins, to facilitate proper folding and pre …
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