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Items: 17

1.

FreeSASA: An open source C library for solvent accessible surface area calculations.

Mitternacht S.

F1000Res. 2016 Feb 18;5:189. doi: 10.12688/f1000research.7931.1.

2.

Mechanical resistance in unstructured proteins.

Jónsson SÆ, Mitternacht S, Irbäck A.

Biophys J. 2013 Jun 18;104(12):2725-32. doi: 10.1016/j.bpj.2013.05.003.

3.

SPACER: Server for predicting allosteric communication and effects of regulation.

Goncearenco A, Mitternacht S, Yong T, Eisenhaber B, Eisenhaber F, Berezovsky IN.

Nucleic Acids Res. 2013 Jul;41(Web Server issue):W266-72. doi: 10.1093/nar/gkt460.

4.

Unraveling hidden regulatory sites in structurally homologous metalloproteases.

Udi Y, Fragai M, Grossman M, Mitternacht S, Arad-Yellin R, Calderone V, Melikian M, Toccafondi M, Berezovsky IN, Luchinat C, Sagi I.

J Mol Biol. 2013 Jul 10;425(13):2330-46. doi: 10.1016/j.jmb.2013.04.009.

PMID:
23583775
5.

Coherent conformational degrees of freedom as a structural basis for allosteric communication.

Mitternacht S, Berezovsky IN.

PLoS Comput Biol. 2011 Dec;7(12):e1002301. doi: 10.1371/journal.pcbi.1002301.

6.

Binding leverage as a molecular basis for allosteric regulation.

Mitternacht S, Berezovsky IN.

PLoS Comput Biol. 2011 Sep;7(9):e1002148. doi: 10.1371/journal.pcbi.1002148.

7.

Monte Carlo study of the formation and conformational properties of dimers of Aβ42 variants.

Mitternacht S, Staneva I, Härd T, Irbäck A.

J Mol Biol. 2011 Jul 8;410(2):357-67. doi: 10.1016/j.jmb.2011.05.014.

PMID:
21616081
8.

A geometry-based generic predictor for catalytic and allosteric sites.

Mitternacht S, Berezovsky IN.

Protein Eng Des Sel. 2011 Apr;24(4):405-9. doi: 10.1093/protein/gzq115.

9.

On the importance of amino acid sequence and spatial proximity of interacting residues for protein folding.

Mitternacht S, Berezovsky IN.

J Biomol Struct Dyn. 2011 Feb;28(4):607-9; discussion 669-674. No abstract available.

PMID:
21142232
10.

Comparing the folding free-energy landscapes of Abeta42 variants with different aggregation properties.

Mitternacht S, Staneva I, Härd T, Irbäck A.

Proteins. 2010 Sep;78(12):2600-8. doi: 10.1002/prot.22775.

PMID:
20589631
11.

Unfolding times for proteins in a force clamp.

Luccioli S, Imparato A, Mitternacht S, Irbäck A, Torcini A.

Phys Rev E Stat Nonlin Soft Matter Phys. 2010 Jan;81(1 Pt 1):010902.

PMID:
20365316
12.

An effective all-atom potential for proteins.

Irbäck A, Mitternacht S, Mohanty S.

PMC Biophys. 2009 Apr 8;2(1):2. doi: 10.1186/1757-5036-2-2.

13.

Changing the mechanical unfolding pathway of FnIII10 by tuning the pulling strength.

Mitternacht S, Luccioli S, Torcini A, Imparato A, Irbäck A.

Biophys J. 2009 Jan;96(2):429-41. doi: 10.1016/j.bpj.2008.09.043.

14.
15.

Differences in solution behavior among four semiconductor-binding peptides.

Mitternacht S, Schnabel S, Bachmann M, Janke W, Irbäck A.

J Phys Chem B. 2007 May 3;111(17):4355-60.

PMID:
17411083
16.

Thermal versus mechanical unfolding of ubiquitin.

Irbäck A, Mitternacht S.

Proteins. 2006 Nov 15;65(3):759-66.

PMID:
16955491
17.

Dissecting the mechanical unfolding of ubiquitin.

Irbäck A, Mitternacht S, Mohanty S.

Proc Natl Acad Sci U S A. 2005 Sep 20;102(38):13427-32.

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