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Marine Mammal Science, ISSN 0824-0469, 10/2015, Volume 31, Issue 4, pp. 1594 - 1597
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 03/2018, Volume 115, Issue 10, p. 2267
In contrast to other biopolymers such as RNA, most foldable protein sequences have a single, unique native structure, which is the most stable conformation.... 
Proteins | Deformation | Energy | Protein folding | Ribonucleic acid--RNA | Biopolymers | Free energy | Gene sequencing
Journal Article
Biophysical Journal, ISSN 0006-3495, 09/2014, Volume 107, Issue 5, p. 1040
  A unifying feature of the large number of protein structures is that they fall into a large number of folds, each with the same overall backbone structure.... 
Proteins | Molecular structure | Protein folding | Bootstrap method
Journal Article
Biophysical Journal, ISSN 0006-3495, 09/2014, Volume 107, Issue 5, pp. 1040 - 1041
Journal Article
Angewandte Chemie, ISSN 0044-8249, 05/2018, Volume 130, Issue 20, pp. 5776 - 5780
Efficient and accurate models to predict the fitness of a sequence would be extremely valuable in protein design. We have explored the use of statistical... 
Biophysik | Proteindesign | Berechnungen | Koevolution | Statistische Mechanik | Proteins | Monte Carlo method | Analysis | Protein binding | Design | Sequences | Landscape design | Computer simulation | Protein G | Streptococcal protein G | Statistics | Fitness
Journal Article
Biophysical Journal, ISSN 0006-3495, 12/2013, Volume 105, Issue 12, pp. 2611 - 2612
Journal Article
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 03/2016, Volume 113, Issue 12, p. 3263
  All-atom molecular dynamics simulations now allow us to create movies of proteins folding and unfolding. However, it is difficult to assess the accuracy of... 
Proteins | Accuracy | Microscopy | Simulation | Molecular biology | Experiments
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 10/2018, Volume 115, Issue 40, p. 9929
Proteins that undergo liquid–liquid phase separation (LLPS) have been shown to play a critical role in many physiological functions through formation of... 
Temperature | Computer simulation | Liquid phases | Boundaries | Organelles | Proteins | Temperature effects | Phase boundaries | Phase separation | Critical temperature | Assemblies | Coarsening | Material properties
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 10/2013, Volume 110, Issue 44, pp. 17874 - 17879
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 3/2016, Volume 113, Issue 12, pp. 3263 - 3268
All-atom molecular dynamics simulations now allow us to create movies of proteins folding and unfolding. However, it is difficult to assess the accuracy of the... 
Protein engineering | Parallel pathways | Villin HP35 | GTT WW domain | NuG2 | Microscopy - methods | Mutation | Proteins - chemistry | Protein Folding | Biological Sciences | protein engineering | parallel pathways
Journal Article
Journal of Chemical Theory and Computation, ISSN 1549-9618, 03/2018, Volume 14, Issue 3, p. 1706
Atomistic simulations have recently been shown to be sufficiently accurate to reversibly fold globular proteins and have provided insights into folding... 
Proteins | Diffusion rate | Simulation | Molecular structure | Protein folding | Metastable state | Helices | Dimers | Dimerization | Assembly | Free energy | Folding
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 1/2010, Volume 107, Issue 3, pp. 1088 - 1093
Journal Article