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FoldAmyloid: a method of prediction of amyloidogenic regions from protein sequence

Bioinformatics, 2010-02, Vol.26 (3), p.326-332

2010

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Prediction of amyloidogenic and disordered regions in protein chains

PLoS computational biology, 2006-12, Vol.2 (12), p.e177-e177

2006

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Golden triangle for folding rates of globular proteins

Proceedings of the National Academy of Sciences - PNAS, 2013-01, Vol.110 (1), p.147-150

2013

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Correction: Finkelstein et al. How Can Ice Emerge at 0 °C? Biomolecules 2022, 12 , 981

Biomolecules (Basel, Switzerland), 2023-11, Vol.13 (12), p.1687

2023

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Calculation of Crystal-Solution Dissociation Constants

Biomolecules (Basel, Switzerland), 2022-01, Vol.12 (2), p.147

2022

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FoldUnfold: web server for the prediction of disordered regions in protein chain

Bioinformatics, 2006-12, Vol.22 (23), p.2948-2949

2006

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How Can Ice Emerge at 0 °C?

Biomolecules (Basel, Switzerland), 2022-07, Vol.12 (7), p.981

2022

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Intrinsic disorder in protein interactions: insights from a comprehensive structural analysis

PLoS computational biology, 2009-03, Vol.5 (3), p.e1000316-e1000316

2009

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Contact order revisited: Influence of protein size on the folding rate

Protein science, 2003-09, Vol.12 (9), p.2057-2062

2003

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Physics of Ice Nucleation and Antinucleation: Action of Ice-Binding Proteins

Biomolecules (Basel, Switzerland), 2024-01, Vol.14 (1), p.54

2024

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Different packing of external residues can explain differences in the thermostability of proteins from thermophilic and mesophilic organisms

Bioinformatics, 2007-09, Vol.23 (17), p.2231-2238

2007

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Protein folding problem: enigma, paradox, solution

Biophysical reviews, 2022-12, Vol.14 (6), p.1255-1272

2022

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Correction to “Sublimation Entropy and Dissociation Constants Prediction by Quantitative Evaluation of Molecular Mobility in Crystals”

The journal of physical chemistry letters, 2018-12, Vol.9 (23), p.6883-6883

2018

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Sublimation Entropy and Dissociation Constants Prediction by Quantitative Evaluation of Molecular Mobility in Crystals

The journal of physical chemistry letters, 2017-07, Vol.8 (13), p.2758-2763

2017

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Reduction of the Search Space for the Folding of Proteins at the Level of Formation and Assembly of Secondary Structures: A New View on the Solution of Levinthal's Paradox

Chemphyschem, 2015-11, Vol.16 (16), p.3375-3378

2015

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Clarification to “Protein folding problem: enigma, paradox, solution”

Biophysical reviews, 2023-04, Vol.15 (2), p.161-161

2023

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Backbone Carbonyl Group Basicities Are Related to Gas-Phase Fragmentation of Peptides and Protein Folding

Angewandte Chemie (International ed.), 2007-01, Vol.46 (9), p.1481-1484

2007

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Restrictions to protein folding determined by the protein size

FEBS letters, 2013-06, Vol.587 (13), p.1884-1890

2013

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There and back again: Two views on the protein folding puzzle

Physics of life reviews, 2017-07, Vol.21, p.56-71

2017

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Chain length is the main determinant of the folding rate for proteins with three-state folding kinetics

Proteins, structure, function, and bioinformatics, 2003-05, Vol.51 (2), p.162-166

2003

Volltextzugriff (PDF)

Levinthal's question answered ... again?

Journal of biomolecular structure & dynamics, 2013-09, Vol.31 (9), p.1013-1015

2013

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To be folded or to be unfolded?

Protein science, 2004-11, Vol.13 (11), p.2871-2877

2004

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Entropy capacity determines protein folding

Proteins, structure, function, and bioinformatics, 2006-04, Vol.63 (1), p.144-154

2006

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Comparison of X-ray and NMR structures: Is there a systematic difference in residue contacts between X-ray- and NMR-resolved protein structures?

Proteins, structure, function, and bioinformatics, 2005-07, Vol.60 (1), p.139-147

2005

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ComSin: database of protein structures in bound (complex) and unbound (single) states in relation to their intrinsic disorder

Nucleic acids research, 2010-01, Vol.38 (Database issue), p.D283

2010

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FoldAmyloid: a method of prediction of amyloidogenic regions from protein sequence

Prediction of amyloidogenic and disordered regions in protein chains

Golden triangle for folding rates of globular proteins

Correction: Finkelstein et al. How Can Ice Emerge at 0 °C? Biomolecules 2022, 12 , 981

Calculation of Crystal-Solution Dissociation Constants

FoldUnfold: web server for the prediction of disordered regions in protein chain

How Can Ice Emerge at 0 °C?

Intrinsic disorder in protein interactions: insights from a comprehensive structural analysis

Contact order revisited: Influence of protein size on the folding rate

Physics of Ice Nucleation and Antinucleation: Action of Ice-Binding Proteins

Different packing of external residues can explain differences in the thermostability of proteins from thermophilic and mesophilic organisms

Protein folding problem: enigma, paradox, solution

Correction to “Sublimation Entropy and Dissociation Constants Prediction by Quantitative Evaluation of Molecular Mobility in Crystals”

Sublimation Entropy and Dissociation Constants Prediction by Quantitative Evaluation of Molecular Mobility in Crystals

Reduction of the Search Space for the Folding of Proteins at the Level of Formation and Assembly of Secondary Structures: A New View on the Solution of Levinthal's Paradox

Clarification to “Protein folding problem: enigma, paradox, solution”

Backbone Carbonyl Group Basicities Are Related to Gas-Phase Fragmentation of Peptides and Protein Folding

Restrictions to protein folding determined by the protein size

There and back again: Two views on the protein folding puzzle

Chain length is the main determinant of the folding rate for proteins with three-state folding kinetics

Levinthal's question answered ... again?

To be folded or to be unfolded?

Entropy capacity determines protein folding

Comparison of X-ray and NMR structures: Is there a systematic difference in residue contacts between X-ray- and NMR-resolved protein structures?

ComSin: database of protein structures in bound (complex) and unbound (single) states in relation to their intrinsic disorder

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