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Hladílková, Jana, Callisen, Thomas H., Lund, Mikael (2016) Lateral Protein–Protein Interactions at Hydrophobic and Charged Surfaces as a Function of pH and Salt Concentration. The Journal of Physical Chemistry B, 120 (13). 3303-3310 doi:10.1021/acs.jpcb.5b12225

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Reference TypeJournal (article/letter/editorial)
TitleLateral Protein–Protein Interactions at Hydrophobic and Charged Surfaces as a Function of pH and Salt Concentration
JournalThe Journal of Physical Chemistry B
AuthorsHladílková, JanaAuthor
Callisen, Thomas H.Author
Lund, MikaelAuthor
Year2016 (April 7)Volume120
Issue13
PublisherAmerican Chemical Society (ACS)
DOIdoi:10.1021/acs.jpcb.5b12225Search in ResearchGate
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Mindat Ref. ID3886309Long-form Identifiermindat:1:5:3886309:9
GUID0
Full ReferenceHladílková, Jana, Callisen, Thomas H., Lund, Mikael (2016) Lateral Protein–Protein Interactions at Hydrophobic and Charged Surfaces as a Function of pH and Salt Concentration. The Journal of Physical Chemistry B, 120 (13). 3303-3310 doi:10.1021/acs.jpcb.5b12225
Plain TextHladílková, Jana, Callisen, Thomas H., Lund, Mikael (2016) Lateral Protein–Protein Interactions at Hydrophobic and Charged Surfaces as a Function of pH and Salt Concentration. The Journal of Physical Chemistry B, 120 (13). 3303-3310 doi:10.1021/acs.jpcb.5b12225
In(2016, April) The Journal of Physical Chemistry B Vol. 120 (13) American Chemical Society (ACS)

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Pasquier, Coralie, Vazdar, Mario, Forsman, Jan, Jungwirth, Pavel, Lund, Mikael (2017) Anomalous Protein–Protein Interactions in Multivalent Salt Solution. The Journal of Physical Chemistry B, 121 (14). 3000-3006 doi:10.1021/acs.jpcb.7b01051
Li, Weimin, Persson, Björn A., Lund, Mikael, Bergenholtz, Johan, Zackrisson Oskolkova, Malin (2016) Concentration-Induced Association in a Protein System Caused by a Highly Directional Patch Attraction. The Journal of Physical Chemistry B, 120 (34). 8953-8959 doi:10.1021/acs.jpcb.6b06873
Evers, Chris H.J., Andersson, Thorbjörn, Lund, Mikael, Skepö, Marie (2012) Adsorption of Unstructured Protein β-Casein to Hydrophobic and Charged Surfaces. Langmuir, 28. 11843-11849 doi:10.1021/la300892p
Luan, Binquan, Huynh, Tien, Zhou, Ruhong (2016) Potential Interference of Protein–Protein Interactions by Graphyne. The Journal of Physical Chemistry B, 120 (9). 2124-2131 doi:10.1021/acs.jpcb.5b11449
Rösgen, Jörg, Auton, Matthew (2016) Comment on “Osmolyte Effects on Monoclonal Antibody Stability and Concentration-Dependent Protein Interactions with Water and Common Osmolytes”. The Journal of Physical Chemistry B, 120 (43). 11331-11332 doi:10.1021/acs.jpcb.6b05602
Zhang, Yi, Vuković, Lela, Rudack, Till, Han, Wei, Schulten, Klaus (2016) Recognition of Poly-Ubiquitins by the Proteasome through Protein Refolding Guided by Electrostatic and Hydrophobic Interactions. The Journal of Physical Chemistry B, 120 (33). 8137-8146 doi:10.1021/acs.jpcb.6b01327
Zhang, Yi, Vuković, Lela, Rudack, Till, Han, Wei, Schulten, Klaus (2016) Correction to “Recognition of Poly-Ubiquitins by the Proteasome through Protein Refolding Guided by Electrostatic and Hydrophobic Interactions”. The Journal of Physical Chemistry B, 120 (40). 10614 doi:10.1021/acs.jpcb.6b09316
Baveghems, Clive L., Pattammattel, Ajith, Kumar, Challa V. (2016) Designer Histone Complexes: Controlling Protein–DNA Interactions with Protein Charge as an “All-or-None” Digital Switch. The Journal of Physical Chemistry B, 120 (46). 11880-11887 doi:10.1021/acs.jpcb.6b08651
Barnett, Gregory V., Razinkov, Vladimir I., Kerwin, Bruce A., Blake, Steven, Qi, Wei, Curtis, Robin A., Roberts, Christopher J. (2016) Osmolyte Effects on Monoclonal Antibody Stability and Concentration-Dependent Protein Interactions with Water and Common Osmolytes. The Journal of Physical Chemistry B, 120 (13). 3318-3330 doi:10.1021/acs.jpcb.6b00621
Markiewicz, Beatrice N., Mukherjee, Debopreeti, Troxler, Thomas, Gai, Feng (2016) Utility of 5-Cyanotryptophan Fluorescence as a Sensitive Probe of Protein Hydration. The Journal of Physical Chemistry B, 120 (5). 936-944 doi:10.1021/acs.jpcb.5b12233
Palese, Luigi L. (2016) Protein States as Symmetry Transitions in the Correlation Matrices. The Journal of Physical Chemistry B, 120 (44). 11428-11435 doi:10.1021/acs.jpcb.6b09216
 
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