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Chemical Communications (Cambridge, England)|July 18, 2002
What can atomic force microscopy tell us about protein folding?Robert B Best, Jane ClarkeJournal of Molecular Biology|May 7, 2005
What contributions to protein side-chain dynamics are probed by NMR experiments? A molecular dynamics simulation analysisRobert B Best, Jane Clarke, Martin KarplusJournal of the American Chemical Society|June 24, 2004
The origin of protein sidechain order parameter distributionsRobert B Best, Jane Clarke, Martin KarplusJournal of Molecular Biology|November 24, 2007
Crosstalk between the protein surface and hydrophobic core in a core-swapped fibronectin type III domainKate S Billings, Robert B Best, Trevor J Rutherford, et al.Proceedings of the National Academy of Sciences of the United States of America|September 10, 2002
A simple method for probing the mechanical unfolding pathway of proteins in detailRobert B Best, Susan B Fowler, Jose L Toca-Herrera, et al.Biochemistry|February 6, 2004
Hydrophobic core fluidity of homologous protein domains: relation of side-chain dynamics to core composition and packingRobert B Best, Trevor J Rutherford, Stefan M V Freund, et al.Biophysical Journal|April 11, 2006
Structural comparison of the two alternative transition states for folding of TI I27Christian D Geierhaas, Robert B Best, Emanuele Paci, et al.Journal of Molecular Biology|July 10, 2003
Mechanical unfolding of a titin Ig domain: structure of transition state revealed by combining atomic force microscopy, protein engineering and molecular dynamics simulationsRobert B Best, Susan B Fowler, José L Toca Herrera, et al.Nature|May 31, 2011
Single-molecule fluorescence reveals sequence-specific misfolding in multidomain proteinsMadeleine B Borgia, Alessandro Borgia, Robert B Best, et al.Nature|March 28, 2003
Hidden complexity in the mechanical properties of titinPhilip M Williams, Susan B Fowler, Robert B Best, et al.Pageof 28