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1
Urea denaturation by stronger dispersion interactions with proteins than water implies a 2-stage unfolding
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Urea denaturation by stronger dispersion interactions with proteins than water implies a 2-stage unfolding

Hua, Lan ; Zhou, Ruhong ; Thirumalai, D ; Berne, B.J

Proceedings of the National Academy of Sciences - PNAS, 2008-11, Vol.105 (44), p.16928-16933 [Periódico revisado por pares]

United States: National Academy of Sciences

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2
pH-induced molecular shedding drives the formation of amyloid fibril-derived oligomers
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pH-induced molecular shedding drives the formation of amyloid fibril-derived oligomers

Tipping, Kevin W. ; Karamanos, Theodoros K. ; Jakhria, Toral ; Iadanza, Matthew G. ; Goodchild, Sophia C. ; Tuma, Roman ; Ranson, Neil A. ; Hewitt, Eric W. ; Radford, Sheena E.

Proceedings of the National Academy of Sciences - PNAS, 2015-05, Vol.112 (18), p.5691-5696 [Periódico revisado por pares]

United States: National Academy of Sciences

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3
Role of clusters in nonclassical nucleation and growth of protein crystals
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Role of clusters in nonclassical nucleation and growth of protein crystals

Sleutel, Mike ; Van Driessche, Alexander E. S.

Proceedings of the National Academy of Sciences - PNAS, 2014-02, Vol.111 (5), p.1674-1674 [Periódico revisado por pares]

United States: National Academy of Sciences

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4
Protein aggregation in salt solutions
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Protein aggregation in salt solutions

Kastelic, Miha ; Kalyuzhnyi, Yurij V. ; Hribar-Lee, Barbara ; Dill, Ken A. ; Vlachy, Vojko

Proceedings of the National Academy of Sciences - PNAS, 2015-05, Vol.112 (21), p.6766-6770 [Periódico revisado por pares]

United States: National Academy of Sciences

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5
On achieving high accuracy and reliability in the calculation of relative protein–ligand binding affinities
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On achieving high accuracy and reliability in the calculation of relative protein–ligand binding affinities

Wang, Lingle ; Berne, B. J. ; Friesner, Richard A.

Proceedings of the National Academy of Sciences - PNAS, 2012-02, Vol.109 (6), p.1937-1942 [Periódico revisado por pares]

United States: National Academy of Sciences

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6
inverse and direct Hofmeister series for lysozyme
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inverse and direct Hofmeister series for lysozyme

Zhang, Yanjie ; Cremer, Paul S

Proceedings of the National Academy of Sciences - PNAS, 2009-09, Vol.106 (36), p.15249-15253 [Periódico revisado por pares]

United States: National Academy of Sciences

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7
Critical structural fluctuations of proteins upon thermal unfolding challenge the Lindemann criterion
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Critical structural fluctuations of proteins upon thermal unfolding challenge the Lindemann criterion

Katava, Marina ; Stirnemann, Guillaume ; Zanatta, Marco ; Capaccioli, Simone ; Pachetti, Maria ; Ngai, K. L. ; Sterpone, Fabio ; Paciaroni, Alessandro

Proceedings of the National Academy of Sciences - PNAS, 2017-08, Vol.114 (35), p.9361-9366 [Periódico revisado por pares]

United States: National Academy of Sciences

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8
Energy landscape in protein folding and unfolding
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Energy landscape in protein folding and unfolding

Mallamace, Francesco ; Corsaro, Carmelo ; Mallamace, Domenico ; Vasi, Sebastiano ; Vasi, Cirino ; Baglioni, Piero ; Buldyrev, Sergey V. ; Chen, Sow-Hsin ; Stanley, H. Eugene

Proceedings of the National Academy of Sciences - PNAS, 2016-03, Vol.113 (12), p.3159-3163 [Periódico revisado por pares]

United States: National Academy of Sciences

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9
How internal cavities destabilize a protein
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How internal cavities destabilize a protein

Xue, Mengjun ; Wakamoto, Takuro ; Kejlberg, Camilla ; Yoshimura, Yuichi ; Nielsen, Tania Aaquist ; Risør, Michael Wulff ; Sanggaard, Kristian Wejse ; Kitahara, Ryo ; Mulder, Frans A. A.

Proceedings of the National Academy of Sciences - PNAS, 2019-10, Vol.116 (42), p.21031-21036 [Periódico revisado por pares]

United States: National Academy of Sciences

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10
Conformational selection and adaptation to ligand binding in T4 lysozyme cavity mutants
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Conformational selection and adaptation to ligand binding in T4 lysozyme cavity mutants

López, Carlos J ; Yang, Zhongyu ; Altenbach, Christian ; Hubbell, Wayne L

Proceedings of the National Academy of Sciences - PNAS, 2013-11, Vol.110 (46), p.E4306-E4315 [Periódico revisado por pares]

United States: National Academy of Sciences

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