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Annual Review of Biophysics, ISSN 1936-122X, 5/2018, Volume 47, Issue 1, pp. 19 - 39
Proteins can collapse into compact globules or form expanded, solvent-accessible, coil-like conformations. Additionally, they can fold into well-defined... 
solvent quality | unfolded states | polymer physics | intrinsically disordered proteins | collapse | Protein research | Protein-protein interactions | Research
Journal Article
Biophysical Journal, ISSN 0006-3495, 02/2018, Volume 114, Issue 3, pp. 4a - 4a
Journal Article
Biophysical Journal, ISSN 0006-3495, 02/2019, Volume 116, Issue 3, pp. 179a - 179a
Journal Article
Biophysical Journal, ISSN 0006-3495, 02/2019, Volume 116, Issue 3, p. 200
Journal Article
Journal Article
eLife, ISSN 2050-084X, 11/2017, Volume 6
Phase transitions of linear multivalent proteins control the reversible formation of many intracellular membraneless bodies. Specific non-covalent crosslinks... 
RNA-POLYMERASE-II | THERMOREVERSIBLE GELATION | SEQUENCE-ENSEMBLE RELATIONSHIPS | LOW-COMPLEXITY DOMAINS | 3-DIMENSIONAL POLYMERS | DESIGNED PEPTIDE | BIOLOGY | INTERACTION NETWORKS | MOLECULAR-SIZE DISTRIBUTION | C-TERMINAL DOMAIN | MONTE-CARLO SIMULATIONS | Proteins | Simulation | Gels | Gelation | Ligands | Mathematical models | Polymers | Phase transitions
Journal Article
Nature Materials, ISSN 1476-1122, 10/2015, Volume 14, Issue 11, pp. 1083 - 1084
  Proteins can undergo reversible phase transitions in response to stimuli. These include changes in temperature, mechanical stress, pH and amino acid sequence... 
Repetitive Sequences, Amino Acid - genetics | Sequence Analysis, Protein - methods | Proteome - genetics | Animals | Proteome - chemistry | Humans | Proteins | Amino acids | Temperature | Polymers
Journal Article
Journal of the American Chemical Society, ISSN 0002-7863, 11/2016, Volume 138, Issue 47, pp. 15323 - 15335
Many cell signaling events are coordinated by intrinsically disordered protein regions (IDRs) that undergo multisite Serine/Threonine phosphorylation. The... 
TAU-PROTEIN | CHEMICAL-SHIFTS | NMR-SPECTROSCOPY | RAY SOLUTION SCATTERING | S-PHASE | SWITCH | SACCHAROMYCES-CEREVISIAE | POLYPROLINE | PROLINE | CHEMISTRY, MULTIDISCIPLINARY | CHAIN EXPANSION | Proteins | Molecular simulation | Phosphorylation | Usage | Chemical properties | Research
Journal Article
Science, ISSN 0036-8075, 01/2018, Volume 359, Issue 6371, pp. 47 - 47
Journal Article
Biophysical Journal, ISSN 0006-3495, 02/2019, Volume 116, Issue 3, pp. 178a - 178a
Journal Article
Biophysical Journal, ISSN 0006-3495, 02/2019, Volume 116, Issue 3, p. 194
Journal Article
Biophysical Journal, ISSN 0006-3495, 02/2019, Volume 116, Issue 3, p. 349
Journal Article
Biophysical Journal, ISSN 0006-3495, 09/2017, Volume 113, Issue 5, pp. 971 - 973
Journal Article
NATURE CHEMISTRY, ISSN 1755-4330, 11/2017, Volume 9, Issue 11, pp. 1118 - 1125
Journal Article
Cell, ISSN 0092-8674, 07/2018, Volume 174, Issue 3, pp. 688 - 699.e16
Journal Article
Biophysical Journal, ISSN 0006-3495, 02/2018, Volume 114, Issue 3, pp. 79a - 79a
Journal Article
Cell, ISSN 0092-8674, 10/2017, Volume 171, Issue 3, pp. 499 - 500
The low-complexity domain (LCD) of the FUS protein forms concentration-dependent assemblies, including liquid droplets and fibril-based hydrogels. The... 
HYDROGELS | DOMAINS | BIOCHEMISTRY & MOLECULAR BIOLOGY | PHASE-TRANSITION | MUTATION | CELL BIOLOGY | RNA-Binding Protein FUS | Analysis | Biomedical engineering
Journal Article
NATURE MATERIALS, ISSN 1476-1122, 11/2015, Volume 14, Issue 11, pp. 1083 - 1084
Journal Article
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