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1. Full Text Role of solvation effects in protein denaturation: From thermodynamics to single molecules and back
by England, Jeremy L and Haran, Gilad
Annual Review of Physical Chemistry, ISSN 0066-426X, 05/2011, Volume 62, Issue 1, pp. 257 - 277
Protein stability often is studied in vitro through the use of urea and guanidinium chloride, chemical cosolvents that disrupt protein native structure. Much... 
molecular dynamics simulations | single-molecule spectroscopy | guanidinium chloride | FRET | protein folding | hydrophobic effect | urea | COIL-GLOBULE TRANSITION | CHEMISTRY, PHYSICAL | UNFOLDED PROTEINS | HYDROPHOBIC COLLAPSE | TRANSFER MODEL | CHAIN | AQUEOUS UREA SOLUTIONS | GUANIDINIUM CHLORIDE SOLUTIONS | AMINO-ACIDS | PHASE-TRANSITION | DYNAMICS | Protein Denaturation - drug effects | Guanidine - chemistry | Hydrophobic and Hydrophilic Interactions - drug effects | Solvents - chemistry | Guanidine - pharmacology | Protein Conformation - drug effects | Molecular Dynamics Simulation | Urea - chemistry | Solvents - pharmacology | Thermodynamics | Protein Folding - drug effects | Protein Structure, Secondary - drug effects | Water - chemistry | Fluorescence Resonance Energy Transfer - methods | Proteins - chemistry | Urea - pharmacology | Proteins | Molecular dynamics | Solvation | Research | Denaturation
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2. Full Text Effect of Urea on the β-Hairpin Conformational Ensemble and Protein Denaturation Mechanism
by Berteotti, Anna and Barducci, Alessandro and Parrinello, Michele
Journal of the American Chemical Society, ISSN 0002-7863, 11/2011, Volume 133, Issue 43, pp. 17200 - 17206
Despite the daily use of urea to influence protein folding and stability, the molecular mechanism with which urea acts is still not well understood. Here the... 
SINGLE-MOLECULE FRET | HYDROPHOBIC INTERACTIONS | WELL-TEMPERED METADYNAMICS | DYNAMICS | UNFOLDED PROTEINS | SIMULATIONS | BACKBONE | GUANIDINIUM CHLORIDE | WATER-STRUCTURE | CHEMISTRY, MULTIDISCIPLINARY | PEPTIDE | Protein Denaturation - drug effects | Protein Conformation - drug effects | Urea - pharmacology | Bacterial Proteins - chemistry | Water - chemistry
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3. Full Text Backbone and Side-Chain Contributions in Protein Denaturation by Urea
by Canchi, Deepak R and García, Angel E
Biophysical Journal, ISSN 0006-3495, 2011, Volume 100, Issue 6, pp. 1526 - 1533
Urea is a commonly used protein denaturant, and it is of great interest to determine its interaction with various protein groups to elucidate the molecular... 
PREFERENTIAL INTERACTIONS | TRIMETHYLAMINE-N-OXIDE | ACCESSIBLE SURFACE-AREAS | THERMODYNAMICS | BIOPHYSICS | TRP-CAGE MINIPROTEIN | MOLECULAR-DYNAMICS METHOD | FORCE-FIELD | MODEL | SIMULATION | WATER | Dose-Response Relationship, Drug | Protein Denaturation - drug effects | Temperature | Hydrogen Bonding | Peptides - chemistry | Protein Folding - drug effects | Molecular Dynamics Simulation | Urea - pharmacology | Protein
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4. Full Text Overview of the Stability of α-Chymotrypsin in Different Solvent Media
by Kumar, Awanish and Venkatesu, Pannuru
Chemical Reviews, ISSN 0009-2665, 07/2012, Volume 112, Issue 7, pp. 4283 - 4307
UREA-INDUCED DENATURATION | LOW PH DIMERIZATION | TRIMETHYLAMINE N-OXIDE | SODIUM DODECYL-SULFATE | NATURALLY-OCCURRING OSMOLYTES | LOW WATER ACTIVITY | X-RAY-DIFFRACTION | IRREVERSIBLE THERMO-INACTIVATION | CATALYTIC-ACTIVITY | CHEMISTRY, MULTIDISCIPLINARY | GUANIDINE-HYDROCHLORIDE DENATURATION | Ionic Liquids - pharmacology | Protein Denaturation - drug effects | Animals | Humans | Chymotrypsin - chemistry | Enzyme Stability - drug effects | Osmosis - drug effects | Solvents - pharmacology
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5. Full Text ATP as a biological hydrotrope
by Patel, A and Malinovska, L and Saha, S and Wang, J and Alberti, S and Krishnan, Y and Hyman, AA
SCIENCE, ISSN 0036-8075, 05/2017, Volume 356, Issue 6339, pp. 753 - 756
Hydrotropes are small molecules that solubilize hydrophobic molecules in aqueous solutions. Typically, hydrotropes are amphiphilic molecules and differ from... 
PREFERENTIAL HYDRATION | SOLUBILIZATION | PROTEIN | MECHANISM | FUS | BEHAVIOR | MULTIDISCIPLINARY SCIENCES | PHASE-TRANSITION | CYTOPLASM | STRESS | GRANULES | Adenosine Triphosphate - pharmacology | Solubility - drug effects | Protein Denaturation - drug effects | Solutions | Models, Biological | Protein Stability - drug effects | Hydrophobic and Hydrophilic Interactions | Protein Aggregates - drug effects | Physiological aspects | Muscle proteins | Adenosine triphosphate | Proteins | Aqueous solutions | Energy | Phase separation | Liquid phases | Solubility | Energy sources | Cooperativity | Hydrophobicity | Surfactants | Protein interaction
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6. Full Text Osmolyte Counteracts Urea-Induced Denaturation of α-Chymotrypsin
by Venkatesu, Pannur and Lee, Ming-Jer and Lin, Ho-mu
The Journal of Physical Chemistry B, ISSN 1520-6106, 04/2009, Volume 113, Issue 15, pp. 5327 - 5338
The stability of proteins is reduced by urea, which is methylamine and nonprotecting osmolyte; eventually urea destabilizes the activity and function and... 
B: Biophysical Chemistry | MOLECULAR-MECHANISM | TRIMETHYLAMINE-N-OXIDE | PROTEIN STABILITY | OSMOTIC-STRESS | SERINE PROTEASES | HUMAN SERUM-ALBUMIN | GUANIDINE-HYDROCHLORIDE | CHEMISTRY, PHYSICAL | SOLVATION DYNAMICS | ORGANIC MEDIA | WATER | Protein Structure, Tertiary | Protein Denaturation - drug effects | Temperature | Urea - chemistry | Thermodynamics | Light | Chymotrypsin - chemistry | Calorimetry, Differential Scanning | Protein Conformation | Scattering, Radiation | Methylamines - chemistry | Methylamines - pharmacology | Urea - pharmacology
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7. Full Text Tunable Inhibition and Denaturation of α-Chymotrypsin with Amino Acid-Functionalized Gold Nanoparticles
by You, Chang-Cheng and De, Mrinmoy and Han, Gang and Rotello, Vincent M
Journal of the American Chemical Society, ISSN 0002-7863, 09/2005, Volume 127, Issue 37, pp. 12873 - 12881
Water-soluble gold nanoparticles bearing diverse l-amino acid terminals have been fabricated to probe the effect of receptor surface on protein surface... 
CLUSTER MOLECULES | MIXED MONOLAYER | SELF-ASSEMBLED MONOLAYERS | BUILDING-BLOCKS | SURFACE RECOGNITION | PROTEIN-PROTEIN INTERACTIONS | HIV-1 PROTEASE | RECEPTORS | BINDING | CHEMISTRY, MULTIDISCIPLINARY | PEPTIDE | Gold - chemistry | Protein Denaturation - drug effects | Amino Acids - chemistry | Models, Molecular | Amino Acids - chemical synthesis | Amino Acids - pharmacology | Binding, Competitive - drug effects | Particle Size | Time Factors | Surface Properties | Chymotrypsin - antagonists & inhibitors | Chymotrypsin - chemistry | Nanostructures - chemistry | Ligands | Molecular Structure | Kinetics | Circular Dichroism | Nanoparticles | Chymotrypsin | Amino acids | Gold compounds | Chemical properties | Research
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8. Full Text On the mechanism of SDS‐induced protein denaturation
by Bhuyan, Abani K
Biopolymers, ISSN 0006-3525, 02/2010, Volume 93, Issue 2, pp. 186 - 199
To understand the mechanism of ionic detergent‐induced protein denaturation, this study examines the action of sodium dodecyl sulfate on ferrocytochrome c... 
protein chain expansion | cytochrome c | necklace model | SDS‐protein interaction | SDS unfolding | Cytochrome c | SDS-protein interaction | Protein chain expansion | Necklace model | HUMAN ALPHA-SYNUCLEIN | MOLTEN GLOBULE STATE | BIOCHEMISTRY & MOLECULAR BIOLOGY | GUANIDINE-HYDROCHLORIDE | HORSE CYTOCHROME-C | FERRICYTOCHROME-C | POLYACRYLAMIDE GEL-ELECTROPHORESIS | BIOPHYSICS | SODIUM DODECYL-SULFATE | AMINO-ACIDS | SURFACTANT INTERACTIONS | ANGLE NEUTRON-SCATTERING | Cytochromes c - chemistry | Protein Structure, Tertiary | Detergents - pharmacology | Protein Denaturation - drug effects | Heme - chemistry | Oxidation-Reduction | Protein Structure, Secondary | Micelles | Sodium Dodecyl Sulfate - pharmacology | Models, Molecular | Spectrophotometry | Hydrogen-Ion Concentration
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9. Full Text Protein Folding Kinetics:  Barrier Effects in Chemical and Thermal Denaturation Experiments
by Naganathan, Athi N and Doshi, Urmi and Muñoz, Victor
Journal of the American Chemical Society, ISSN 0002-7863, 05/2007, Volume 129, Issue 17, pp. 5673 - 5682
Recent experimental work on fast protein folding brings about an intriguing paradox. Microsecond-folding proteins are supposed to fold near or at the folding... 
SPEED LIMIT | SIMPLE-MODEL | WW DOMAIN | HELIX FORMATION | FREE-ENERGY BARRIERS | DYNAMICS | TRANSITION-STATE | DIFFUSION | 3-HELIX BUNDLE PROTEIN | DOWNHILL | CHEMISTRY, MULTIDISCIPLINARY | Protein Denaturation - drug effects | Thermodynamics | Temperature | Algorithms | Models, Chemical | Computer Simulation | Surface Properties | Entropy | Energy Transfer | Kinetics | Protein Folding | Proteins | Research | Protein folding | Denaturation
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10. Full Text Quantitative Assessments of the Distinct Contributions of Polypeptide Backbone Amides versus Side Chain Groups to Chain Expansion via Chemical Denaturation
by Holehouse, Alex S and Garai, Kanchan and Lyle, Nicholas and Vitalis, Andreas and Pappu, Rohit V
Journal of the American Chemical Society, ISSN 0002-7863, 03/2015, Volume 137, Issue 8, pp. 2984 - 2995
In aqueous solutions with high concentrations of chemical denaturants such as urea and guanidinium chloride (GdmCl) proteins expand to populate heterogeneous... 
COMPACT UNFOLDED STATE | INTRINSICALLY DISORDERED PROTEINS | UREA SOLUTIONS | MOLECULAR-DYNAMICS | AQUEOUS GUANIDINIUM CHLORIDE | SOLVENT POLYMER-SOLUTIONS | NONNATIVE STRUCTURE | FORCE-FIELD | POTENTIAL FUNCTIONS | FLUORESCENCE CORRELATION SPECTROSCOPY | CHEMISTRY, MULTIDISCIPLINARY | Dose-Response Relationship, Drug | Amino Acid Sequence | Protein Denaturation - drug effects | Peptides - chemistry | Protein Structure, Secondary | Guanidine - pharmacology | Water - chemistry | Amides - chemistry | Hydrophobic and Hydrophilic Interactions | Molecular Sequence Data | Molecular Dynamics Simulation | Urea - pharmacology | Molecular dynamics | Polypeptides | Aqueous solution reactions | Analysis
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11. Full Text Influence of calcium on β-lactoglobulin denaturation kinetics: Implications in unfolding and aggregation mechanisms
by Petit, J and Herbig, A.-L and Moreau, A and Delaplace, G
Journal of Dairy Science, ISSN 0022-0302, 12/2011, Volume 94, Issue 12, pp. 5794 - 5810
Much research dealing with the processing of milk by-products in heat exchangers has noted the key role of calcium in β-lactoglobulin (β-LG) fouling behavior.... 
thermodynamics | calcium | heat denaturation | β-lactoglobulin | Heat denaturation | Thermodynamics | Calcium | AGRICULTURE, DAIRY & ANIMAL SCIENCE | THERMAL-DENATURATION | FOOD SCIENCE & TECHNOLOGY | WHEY-PROTEIN | HIGH-TEMPERATURE | DEPOSIT FORMATION | beta-lactoglobulin | CONCENTRATE | HEAT-EXCHANGERS | STEEL SURFACES | ALPHA-LACTALBUMIN | INDUCED STRUCTURAL-CHANGES | MILK | Dose-Response Relationship, Drug | Lactoglobulins - drug effects | Protein Denaturation - drug effects | Animals | Calcium - pharmacology | Cattle | Protein Unfolding - drug effects | Chromatography, High Pressure Liquid | Hot Temperature | Lactoglobulins - chemistry
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12. Full Text Protein destabilisation in ionic liquids: The role of preferential interactions in denaturation
by Figueiredo, Angelo Miguel and Sardinha, Joao and Moore, Geoffrey R and Cabrita, Eurico J
Physical Chemistry Chemical Physics, ISSN 1463-9076, 12/2013, Volume 15, Issue 45, pp. 19632 - 19643
The preferential binding of anions and cations in aqueous solutions of the ionic liquids (ILs) 1-butyl-3-methylimidazolium ([C(4)mim](+)) and... 
BACKBONE DYNAMICS | PEPTIDE GROUP | CYTOCHROME-C | MAGNETIC-RESONANCE RELAXATION | ON-PATHWAY INTERMEDIATE | AQUEOUS-SOLUTIONS | 1-BUTYL-3-METHYLIMIDAZOLIUM CHLORIDE | PHYSICS, ATOMIC, MOLECULAR & CHEMICAL | CHEMISTRY, PHYSICAL | SECONDARY STRUCTURE | HYDROGEN-EXCHANGE | MODEL-FREE APPROACH | Ionic Liquids - pharmacology | Protein Denaturation - drug effects | Protein Structure, Secondary | Solvents - chemistry | Protein Stability - drug effects | Water - chemistry | Carrier Proteins - chemistry | Imidazoles - pharmacology | Escherichia coli Proteins - chemistry | Molecular Dynamics Simulation | Proteins | Binding | Residues | Anions | Simulation | Denaturation | Ionic liquids | Cations
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13. Full Text Kinetic evidence for a two-stage mechanism of protein denaturation by guanidinium chloride
by Santosh Kumar Jha and Susan Marqusee
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 4/2014, Volume 111, Issue 13, pp. 4856 - 4861
Dry molten globular (DMG) intermediates, an expanded form of the native protein with a dry core, have been observed during denaturant-induced unfolding of many... 
Proteins | Molecules | Thiols | Solvation | Chlorides | Globules | Fluorescence | Data lines | Kinetics | Biopolymer denaturation | Steady-state FRET | Dry molten globule | Protein unfolding | COOPERATIVE TRANSITIONS | UREA SOLUTIONS | protein unfolding | MULTIDISCIPLINARY SCIENCES | EQUILIBRIUM | steady-state FRET | PACKING | INTERMEDIATE | dry molten globule | HYDRATION | MOLECULES | WATER | Protein Denaturation - drug effects | Escherichia coli - enzymology | Protein Structure, Secondary | Sulfhydryl Compounds - pharmacology | Protein Unfolding - drug effects | Solvents - chemistry | Guanidine - pharmacology | Nitrobenzoates - pharmacology | Tryptophan - metabolism | Sulfhydryl Compounds - metabolism | Ribonuclease H - chemistry | Circular Dichroism | Ribonuclease H - metabolism | Protein research | Dichloropropane | Protein folding | Chemical properties | Research | Identification and classification | Biological Sciences | Physical Sciences
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14. Full Text Denaturation via Surfactants Changes Composition of Protein Corona
by Müller, Julius and Simon, Johanna and Rohne, Philipp and Koch-Brandt, Claudia and Mailänder, Volker and Morsbach, Svenja and Landfester, Katharina
Biomacromolecules, ISSN 1525-7797, 07/2018, Volume 19, Issue 7, pp. 2657 - 2664
The use of nanocarriers as drug delivery vehicles brings them into contact with blood plasma proteins. Polymeric nanocarriers require some sort of surfactant... 
NANOPARTICLES | POLYMER SCIENCE | SODIUM DODECYL-SULFATE | MINIEMULSION POLYMERIZATION | STABILITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | CHEMISTRY, ORGANIC | ADSORPTION | BINDING | BOVINE SERUM-ALBUMIN | Protein Corona - chemistry | Protein Denaturation - drug effects | Surface-Active Agents - chemistry | Cetrimonium - chemistry | Cetrimonium - pharmacology | Surface-Active Agents - pharmacology
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15. Full Text Thioflavin T‑Silent Denaturation Intermediates Support the Main-Chain-Dominated Architecture of Amyloid Fibrils
by Noda, Sayaka and So, Masatomo and Adachi, Masayuki and Kardos, József and Akazawa-Ogawa, Yoko and Hagihara, Yoshihisa and Goto, Yuji
Biochemistry, ISSN 0006-2960, 07/2016, Volume 55, Issue 28, pp. 3937 - 3948
Ultrasonication is considered one of the most effective agitations for inducing the spontaneous formation of amyloid fibrils. When we induced the... 
MOLECULAR-MECHANISM | TRYPTOPHAN MUTAGENESIS | BETA-MICROGLOBULIN | PROTEIN | MOLTEN GLOBULE STATE | BIOCHEMISTRY & MOLECULAR BIOLOGY | COMMON MECHANISM | ALPHA-SYNUCLEIN | ULTRASONICATION | QUANTITATIVE-ANALYSIS | NEURODEGENERATIVE DISEASES | Ultrasonic Waves | Cell Survival - drug effects | Protein Denaturation - drug effects | Protein Structure, Secondary | Guanidine - pharmacology | Humans | Rats | beta 2-Microglobulin - chemistry | Amyloid - chemistry | PC12 Cells | beta 2-Microglobulin - toxicity | Animals | Insulin - chemistry | Thiazoles - chemistry | Protein Aggregates - drug effects | Usage | Glycoproteins | Ultrasonic equipment | Research
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16. Full Text Denaturation induced aggregation in α‐crystallin: differential action of chaotropes
by Khan, Mohd Shahnawaz and Bhat, Sheraz Ahmad and Tabrez, Shams and Alama, Mohammed Nabil and Alsenaidy, Mohammad A and Al‐Senaidy, Abdulrahman M
Journal of Molecular Recognition, ISSN 0952-3499, 11/2016, Volume 29, Issue 11, pp. 536 - 543
α‐Crystallin is a member of small heat shock proteins and is believed to play an exceptional role in the stability of eye lens proteins. The disruption or... 
aggregation | heat shock protein | amyloid | α‐crystallin | guanidine hydrochloride | urea | Aggregation | Guanidine hydrochloride | Urea | Amyloid | α-crystallin | Heat shock protein | STATES | WEIGHT PROTEIN-FRACTIONS | B-CRYSTALLIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | MECHANISMS | TOXICITY | AMYLOID-FIBRIL FORMATION | crystallin | POLYPEPTIDES | BIOPHYSICS | DISEASE | MOLECULAR CHAPERONE | CATARACTOUS HUMAN LENSES | Protein Denaturation - drug effects | alpha-Crystallins - drug effects | Amyloid - metabolism | Protein Structure, Secondary | Guanidine - pharmacology | Hydrophobic and Hydrophilic Interactions | Models, Molecular | alpha-Crystallins - chemistry | Circular Dichroism | Protein Folding | Urea - pharmacology | Proteins | Ellipticity | Chaos theory | Fluorescence | Ureas | Formations | Agglomeration | Doppler effect
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