المؤلفون: Luong, Thinh DN, Nagpal, Suhani, Sadqi, Mourad, Muñoz, Victor

المصدر: Proceedings of the National Academy of Sciences of the United States of America. 119(23)

مصطلحات موضوعية: Biological Sciences, Bioinformatics and Computational Biology, Chemical Sciences, 1.1 Normal biological development and functioning, Generic health relevance, Intrinsically Disordered Proteins, Molecular Conformation, Protein Binding, Protein Conformation, Protein Folding, intrinsically disordered proteins, folding upon binding, folding landscapes, conformational rheostat

وصف الملف: application/pdf

URL الوصول: https://escholarship.org/uc/item/25w0h2x8
https://escholarship.org/content/qt25w0h2x8/qt25w0h2x8.pdf

المؤلفون: Zavrtanik, Uroš, Medved, Tadej, Purič, Samo, Vranken, Wim F., Lah, Jurij, Hadži, San

المصدر: Journal of molecular biology, vol. 436, no. 4, 168444, 2024. ; ISSN: 0022-2836

مصطلحات موضوعية: intrinsically disordered proteins, folding-upon-binding, pre-folding, preotein recognition motif, leucine recognition motif, intrinsic disorder, recognition motif, leucine motif, intrinzično neurejeni proteini, zvitje ob vezanju, prepoznavni motivi, predzvitje, levcinski prepoznavni motivi, info:eu-repo/classification/udc/577.322

وصف الملف: application/pdf; text/url

Relation: https://repozitorij.uni-lj.si/IzpisGradiva.php?id=155238; https://repozitorij.uni-lj.si/Dokument.php?id=185836&dn=; https://repozitorij.uni-lj.si/Dokument.php?id=182035&dn=; https://plus.cobiss.net/cobiss/si/sl/bib/189748995; http://hdl.handle.net/20.500.12556/RUL-155238

الاتاحة: https://repozitorij.uni-lj.si/IzpisGradiva.php?id=155238
https://repozitorij.uni-lj.si/Dokument.php?id=185836&dn=
https://repozitorij.uni-lj.si/Dokument.php?id=182035&dn=
https://plus.cobiss.net/cobiss/si/sl/bib/189748995
https://hdl.handle.net/20.500.12556/RUL-155238

المؤلفون: Noah Giacon, Ettore Lo Cascio, Darcy S. Davidson, Marcelo D. Polêto, Justin A. Lemkul, Valeria Pennacchietti, Livia Pagano, Carlotta Zamparelli, Angelo Toto, Alessandro Arcovito

المصدر: Computational and Structural Biotechnology Journal, Vol 21, Iss , Pp 3259-3271 (2023)

مصطلحات موضوعية: SARS-CoV-2 E protein, Human ZO1-PDZ2 domain, DRUDE force field, Molecular dynamics, Surface Plasmon Resonance, Folding upon binding, Biotechnology, TP248.13-248.65

وصف الملف: electronic resource

Relation: http://www.sciencedirect.com/science/article/pii/S2001037023002106; https://doaj.org/toc/2001-0370

URL الوصول: https://doaj.org/article/5f87ea47f88e4bfda42747021ccdc226

المؤلفون: T. Reid Alderson, Hermann Habacher, Benjamin Bourgeois, Tobias Madl

المصدر: Journal of Magnetic Resonance Open, Vol 12, Iss , Pp 100074- (2022)

مصطلحات موضوعية: LEF-1, Transcription factor, 15N relaxation, Solvent paramagnetic relaxation enhancements, Folding upon binding, Medical physics. Medical radiology. Nuclear medicine, R895-920, Physics, QC1-999

وصف الملف: electronic resource

Relation: http://www.sciencedirect.com/science/article/pii/S2666441022000449; https://doaj.org/toc/2666-4410

URL الوصول: https://doaj.org/article/30914e4031ca4878afee130730318f0d

المؤلفون: Joel Roca-Martinez, Tamas Lazar, Jose Gavalda-Garcia, David Bickel, Rita Pancsa, Bhawna Dixit, Konstantina Tzavella, Pathmanaban Ramasamy, Maite Sanchez-Fornaris, Isel Grau, Wim F. Vranken

المصدر: Frontiers in Molecular Biosciences, Vol 9 (2022)

مصطلحات موضوعية: protein dynamics and conformation, sequence-based prediction, biophysical characteristics, post-translational modification (PTM), deleterious mutation, folding-upon-binding, Biology (General), QH301-705.5

وصف الملف: electronic resource

Relation: https://www.frontiersin.org/articles/10.3389/fmolb.2022.959956/full; https://doaj.org/toc/2296-889X

URL الوصول: https://doaj.org/article/cb1cd7e3a07a4ee9b141fef663760725

المؤلفون: Hadži, San, Lah, Jurij

المصدر: Protein science, vol. 31, no. 7, e4370, 2022. ; ISSN: 0961-8368

مصطلحات موضوعية: binding motif, folding penalty, folding-upon-binding, fuzziness, intrinsically disordered proteins, peptide inhibitor, pre-folding, motiv vezanja, neugodno zvitje, zvitje ob vezanju, kaotičnost, intrinzično neurejeni proteini, peptidni inhibitor, predzvitje, info:eu-repo/classification/udc/577.322

وصف الملف: application/pdf; text/url

Relation: info:eu-repo/grantAgreement/ARRS//J1-1706; info:eu-repo/grantAgreement/ARRS//P1-0201; https://repozitorij.uni-lj.si/IzpisGradiva.php?id=141972; https://repozitorij.uni-lj.si/Dokument.php?id=163817&dn=; https://repozitorij.uni-lj.si/Dokument.php?id=163199&dn=; https://plus.cobiss.net/cobiss/si/sl/bib/121839363; http://hdl.handle.net/20.500.12556/RUL-141972

الاتاحة: https://repozitorij.uni-lj.si/IzpisGradiva.php?id=141972
https://repozitorij.uni-lj.si/Dokument.php?id=163817&dn=
https://repozitorij.uni-lj.si/Dokument.php?id=163199&dn=
https://plus.cobiss.net/cobiss/si/sl/bib/121839363
https://hdl.handle.net/20.500.12556/RUL-141972

المؤلفون: Javeed Ahmad, Mohd Khubaib, Javaid Ahmad Sheikh, Rita Pancsa, Saroj Kumar, Alagiri Srinivasan, Mohan Madan Babu, Seyed E. Hasnain, Nasreen Z. Ehtesham

المصدر: FEBS Open Bio, Vol 10, Iss 1, Pp 70-85 (2020)

مصطلحات موضوعية: folding‐upon‐binding, immune modulation, immunogenicity, Mycobacterium tuberculosis, pathogenesis, protein–protein interaction, Biology (General), QH301-705.5

وصف الملف: electronic resource

Relation: https://doaj.org/toc/2211-5463

URL الوصول: https://doaj.org/article/2fac3cb98bcb4b81b7511515a5e073a3

المؤلفون: Kragelj, Jaka, Orand, Thibault, Delaforge, Elise, Tengo, Laura, Blackledge, Martin, Palencia, Andrés, Jensen, Malene Ringkjøbing

المساهمون: Institut de biologie structurale (IBS - UMR 5075), Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA), Institute for Advanced Biosciences / Institut pour l'Avancée des Biosciences (Grenoble) (IAB), Centre Hospitalier Universitaire CHU Grenoble (CHUGA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Etablissement français du sang - Auvergne-Rhône-Alpes (EFS)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA)

المصدر: ISSN: 2218-273X ; Biomolecules ; https://hal.univ-grenoble-alpes.fr/hal-03433956 ; Biomolecules, 2021, 11 (8), pp.1204. ⟨10.3390/biom11081204⟩.

مصطلحات موضوعية: NMR spectroscopy, chemical exchange saturation transfer (CEST), enthalpy–entropy compensation, folding-upon-binding, intrinsically disordered protein (IDP), isothermal titration calorimetry, mitogen-activated protein kinase (MAPK), MESH: Humans, MESH: JNK Mitogen-Activated Protein Kinases, MESH: Kinetics, MESH: MAP Kinase Kinase 4, MESH: Mitogen-Activated Protein Kinase 14, MESH: Models, Molecular, MESH: Protein Binding, MESH: Protein Conformation, MESH: Protein Folding, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM]

Relation: info:eu-repo/semantics/altIdentifier/pmid/34439869; PUBMED: 34439869; PUBMEDCENTRAL: PMC8391806

الاتاحة: https://hal.univ-grenoble-alpes.fr/hal-03433956
https://hal.univ-grenoble-alpes.fr/hal-03433956v1/document
https://hal.univ-grenoble-alpes.fr/hal-03433956v1/file/Kragelj%20et%20al.%20biomolecules.pdf
https://doi.org/10.3390/biom11081204

المؤلفون: Masaru Hoshino

المصدر: Biophysics and Physicobiology, Vol 17 (2020)

مصطلحات موضوعية: intrinsically disordered proteins, molecular recognition, no folding upon binding, specific binding, interaction with multiple target molecules, Biology (General), QH301-705.5, Physiology, QP1-981, Physics, QC1-999

وصف الملف: electronic resource

Relation: https://doaj.org/toc/2189-4779

URL الوصول: https://doaj.org/article/12d8299889dc48868d20fb2648999fab

المؤلفون: Wicky, Basile I. M., Shammas, Sarah L., Clarke, Jane

المصدر: Proceedings of the National Academy of Sciences of the United States of America, 2017 Sep 01. 114(37), 9882-9887.

URL الوصول: https://www.jstor.org/stable/26487694

المؤلفون: Miskei M., Horvath A., Vendruscolo M., Fuxreiter M.

المساهمون: Miskei, M., Horvath, A., Vendruscolo, M., Fuxreiter, M.

مصطلحات موضوعية: disordered protein, folding upon binding, fuzzy complexe, fuzzy interaction, protein binding

Relation: info:eu-repo/semantics/altIdentifier/wos/WOS:000532698400027; volume:432; issue:7; firstpage:2289; lastpage:2303; numberofpages:15; journal:JOURNAL OF MOLECULAR BIOLOGY; http://hdl.handle.net/11577/3353452

الاتاحة: http://hdl.handle.net/11577/3353452
https://doi.org/10.1016/j.jmb.2020.02.017

المؤلفون: San Hadži, Jurij Lah

المصدر: Protein science, vol. 31, no. 7, e4370, 2022.
Protein science, str. 1-11 : Ilustr., Vol. 31, iss. 7, Jul. 2022
COBISS-ID: 15692293

مصطلحات موضوعية: Protein Conformation, alpha-Helical, peptide inhibitor, Protein Folding, neugodno zvitje, peptidni inhibitor, binding motif, folding penalty, folding-upon-binding, fuzziness, intrinsically disordered proteins, peptide inhibitor, prefolding, folding penalty, kaotičnost, fuzziness, Biochemistry, Intrinsically Disordered Proteins, udc:577.322, zvitje ob vezanju, udc:577, binding motif, predzvitje, motiv vezanja, motiv vezanja, neugodno zvitje, zvitje ob vezanju, kaotičnost, intrinzično neurejeni proteini, peptidni inhibitor, predzvitje, folding-upon-binding, intrinsically disordered proteins, pre-folding, Molecular Biology, Inosine Diphosphate, intrinzično neurejeni proteini, Protein Binding

وصف الملف: application/pdf; text/url

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e883e40f456dc28af3af131f4ce7cf61
https://pubmed.ncbi.nlm.nih.gov/35762718

المؤلفون: Jaka Kragelj, Malene Ringkjøbing Jensen, Thibault Orand, Laura Tengo, Elise Delaforge, Andrés Palencia, Martin Blackledge

المساهمون: Institut de biologie structurale (IBS - UMR 5075), Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA), Institute for Advanced Biosciences / Institut pour l'Avancée des Biosciences (Grenoble) (IAB), Centre Hospitalier Universitaire [Grenoble] (CHU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Etablissement français du sang - Auvergne-Rhône-Alpes (EFS)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA), ANR-17-EURE-0003,CBH-EUR-GS,CBH-EUR-GS(2017), European Project: 264257,EC:FP7:PEOPLE,FP7-PEOPLE-2010-ITN,IDPBYNMR(2010)

المصدر: Biomolecules
Biomolecules, MDPI, 2021, 11 (8), pp.1204. ⟨10.3390/biom11081204⟩
Volume 11
Issue 8
Biomolecules, 2021, 11 (8), pp.1204. ⟨10.3390/biom11081204⟩
Biomolecules, Vol 11, Iss 1204, p 1204 (2021)

مصطلحات موضوعية: Models, Molecular, Protein Folding, MAP Kinase Kinase 4, Protein Conformation, MESH: Protein Folding, Sequence (biology), 010402 general chemistry, Intrinsically disordered proteins, Microbiology, 01 natural sciences, Biochemistry, Article, Mitogen-Activated Protein Kinase 14, MESH: Mitogen-Activated Protein Kinase 14, 03 medical and health sciences, NMR spectroscopy, MESH: Protein Conformation, Humans, MESH: Protein Binding, folding-upon-binding, mitogen-activated protein kinase (MAPK), Protein kinase A, Molecular Biology, 030304 developmental biology, 0303 health sciences, MESH: Humans, MESH: Kinetics, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], Kinase, Chemistry, fungi, JNK Mitogen-Activated Protein Kinases, food and beverages, enthalpy–entropy compensation, Isothermal titration calorimetry, Nuclear magnetic resonance spectroscopy, chemical exchange saturation transfer (CEST), MESH: JNK Mitogen-Activated Protein Kinases, Protein superfamily, QR1-502, 0104 chemical sciences, isothermal titration calorimetry, Kinetics, Enthalpy–entropy compensation, Biophysics, intrinsically disordered protein (IDP), MESH: Models, Molecular, Protein Binding, MESH: MAP Kinase Kinase 4

وصف الملف: application/pdf

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b0cad49032be66c6d22fe4c8921367a4
https://hal.univ-grenoble-alpes.fr/hal-03433956/document

المؤلفون: Liza Dahal, Jeffrey J. Hollins, Jane Clarke, Tristan O.C. Kwan

المساهمون: Dahal, Liza [0000-0002-5600-1673], Clarke, Jane [0000-0002-7921-900X], Apollo - University of Cambridge Repository

المصدر: Journal of Molecular Biology. 430:2468-2477

مصطلحات موضوعية: Models, Molecular, 0301 basic medicine, Circular dichroism, Kinetics, Plasma protein binding, Dissociation (chemistry), Mice, 03 medical and health sciences, Structural Biology, Homologous chromosome, Animals, Amino Acid Sequence, Binding site, Molecular Biology, Peptide sequence, BH3, folding upon binding, Binding Sites, 030102 biochemistry & molecular biology, Chemistry, Circular Dichroism, apoptosis, Peptide Fragments, Protein Structure, Tertiary, Cell biology, Myeloid Cell Leukemia Sequence 1 Protein, 030104 developmental biology, Mutation, affinity, Apoptosis Regulatory Proteins, Protein Binding

وصف الملف: application/pdf

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b1c5d6f11bddc8e74276f86c66a4870d
https://doi.org/10.1016/j.jmb.2018.04.004

المؤلفون: Schneider, Robert, Jensen, Malene Ringkjøbing, Blackledge, Martin

المساهمون: Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS), Institut de biologie structurale (IBS - UMR 5075), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes 2016-2019 (UGA 2016-2019 )-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)

المصدر: Intrinsically Disordered Proteins ; https://hal.univ-grenoble-alpes.fr/hal-02416028 ; Intrinsically Disordered Proteins, Elsevier, pp.139-187, 2019, ⟨10.1016/B978-0-12-816348-1.00005-3⟩

مصطلحات موضوعية: Spectroscopy, Intrinsically disordered proteins, Protein-protein interactions, Folding upon binding, Kinetics, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM]

الاتاحة: https://hal.univ-grenoble-alpes.fr/hal-02416028
https://doi.org/10.1016/B978-0-12-816348-1.00005-3

المؤلفون: Javeed Ahmad, M. Madan Babu, Seyed Ehtesham Hasnain, Alagiri Srinivasan, Nasreen Z. Ehtesham, Rita Pancsa, Javaid A. Sheikh, Mohd Khubaib, Saroj Kumar

المصدر: FEBS Open Bio
FEBS Open Bio, Vol 10, Iss 1, Pp 70-85 (2020)

مصطلحات موضوعية: 0301 basic medicine, Subfamily, Protein family, Proline, Proteome, Virulence, Glutamic Acid, Biology, immunogenicity, Intrinsically disordered proteins, General Biochemistry, Genetics and Molecular Biology, Protein–protein interaction, 03 medical and health sciences, Mice, 0302 clinical medicine, Bacterial Proteins, Mycobacterium tuberculosis, folding‐upon‐binding, Animals, Protein secondary structure, Pathogen, lcsh:QH301-705.5, Cells, Cultured, Research Articles, immune modulation, pathogenesis, Computational Biology, 3. Good health, Cell biology, Mice, Inbred C57BL, 030104 developmental biology, protein–protein interaction, lcsh:Biology (General), 030220 oncology & carcinogenesis, Research Article

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7f0d6eb01e1f6507f421132e0d3d860f
https://pubmed.ncbi.nlm.nih.gov/31643141

المؤلفون: Sluchanko, Nikolai N., Bustos, Diego Martin

مصطلحات موضوعية: Ciencias Biológicas, PROTEIN-PROTEIN INTERACTIONS, Biología Celular, Microbiología, PROTEIN DOMAIN, PROTEIN-PROTEIN INTERACTION NETWORKS, MOLECULAR RECOGNITION, PROTEIN STRUCTURE, INTERACTOME, PHOSPHORYLATION, FOLDING UPON BINDING, CIENCIAS NATURALES Y EXACTAS

وصف الملف: application/pdf

URL الوصول: https://explore.openaire.eu/search/publication?articleId=od______3498::4ce5716087425c4d8640e6bf20be5eb1
https://www.sciencedirect.com/science/article/pii/S1877117319300419

المؤلفون: Martin Blackledge, Malene Ringkjøbing Jensen, Robert Schneider

المساهمون: Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Institut de biologie structurale (IBS - UMR 5075), Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA)-Centre National de la Recherche Scientifique (CNRS), Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS), Institut de biologie structurale (IBS - UMR 5075 ), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)

المصدر: Intrinsically Disordered Proteins
Intrinsically Disordered Proteins, Elsevier, pp.139-187, 2019, ⟨10.1016/B978-0-12-816348-1.00005-3⟩

مصطلحات موضوعية: 0303 health sciences, Intrinsically disordered proteins, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], Chemistry, Protein-protein interactions, Computational biology, Folding upon binding, 010402 general chemistry, 01 natural sciences, 0104 chemical sciences, 03 medical and health sciences, Kinetics, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], Spectroscopy, 030304 developmental biology

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fcecc57978f5c1e3b97a4bcd7fc39e7f
http://hal.univ-grenoble-alpes.fr/hal-02416028

المؤلفون: Dahal, Liza, Kwan, Tristan OC, Hollins, Jeffrey J, Clarke, Jane

مصطلحات موضوعية: BH3, affinity, apoptosis, folding upon binding, kinetics, Amino Acid Sequence, Animals, Apoptosis Regulatory Proteins, Binding Sites, Circular Dichroism, Mice, Models, Molecular, Mutation, Myeloid Cell Leukemia Sequence 1 Protein, Peptide Fragments, Protein Binding, Protein Structure, Tertiary

وصف الملف: Print-Electronic; application/pdf

Relation: https://www.repository.cam.ac.uk/handle/1810/277768

الاتاحة: https://www.repository.cam.ac.uk/handle/1810/277768
https://doi.org/10.17863/CAM.25107

المؤلفون: Jane Clarke, Sarah L. Shammas, Basile I. M. Wicky

المساهمون: Wicky, Basile [0000-0002-2501-7875], Clarke, Jane [0000-0002-7921-900X], Apollo - University of Cambridge Repository

مصطلحات موضوعية: 0301 basic medicine, Protein Folding, Hofmeister series, PPI, Protein Conformation, Kinetics, Static Electricity, electrostatic steering, 010402 general chemistry, Intrinsically disordered proteins, 01 natural sciences, Dissociation (chemistry), Ion, 03 medical and health sciences, Mice, Animals, Humans, Cellular compartment, folding upon binding, Multidisciplinary, Chemistry, Protein Stability, Tumor Suppressor Proteins, Osmolar Concentration, Spectrin, Biological Sciences, 0104 chemical sciences, Intrinsically Disordered Proteins, Solutions, Crystallography, 030104 developmental biology, Ionic strength, Biophysics, Myeloid Cell Leukemia Sequence 1 Protein, Thermodynamics, Apoptosis Regulatory Proteins, Marginal stability, co-solute, Protein Binding

وصف الملف: application/pdf

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e23431a69f849b86c8317738922416b4
https://europepmc.org/articles/PMC5604010/