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Gerald R Grimsley

Showing results (11-20 of 18) with videos related to

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Proteins|July 24, 2009
Increasing protein stability by improving beta-turnsHailong Fu, Gerald R Grimsley, Abbas Razvi, et al.
Biophysical Chemistry|December 19, 2002
Charge-charge interactions are the primary determinants of the pK values of the ionizable groups in Ribonuclease T1C Nick Pace, Beatrice M P Huyghues-Despointes, James M Briggs, et al.
Biophysical Journal|December 11, 2007
Tryptophan fluorescence reveals the presence of long-range interactions in the denatured state of ribonuclease SaRoy W Alston, Mauricio Lasagna, Gerald R Grimsley, et al.
Biophysical Journal|December 11, 2007
Peptide sequence and conformation strongly influence tryptophan fluorescenceRoy W Alston, Mauricio Lasagna, Gerald R Grimsley, et al.
Protein Science : a Publication of the Protein Society|March 4, 2010
Urea denatured state ensembles contain extensive secondary structure that is increased in hydrophobic proteinsC Nick Pace, Beatrice M P Huyghues-Despointes, Hailong Fu, et al.
Journal of Molecular Biology|March 8, 2011
Contribution of hydrophobic interactions to protein stabilityC Nick Pace, Hailong Fu, Katrina Lee Fryar, et al.
Journal of Molecular Biology|January 16, 2003
Charge-charge interactions are key determinants of the pK values of ionizable groups in ribonuclease Sa (pI=3.5) and a basic variant (pI=10.2)Douglas V Laurents, Beatrice M P Huyghues-Despointes, Marta Bruix, et al.
Protein Science : a Publication of the Protein Society|March 5, 2014
Contribution of hydrogen bonds to protein stabilityC Nick Pace, Hailong Fu, Katrina Lee Fryar, et al.
Pageof 2

Showing results (11-20 of 18) with videos related to

Sort By:
Pageof 2
You have reached the last page of results.This site can display upto 18 results.
Proteins|July 24, 2009
Increasing protein stability by improving beta-turnsHailong Fu, Gerald R Grimsley, Abbas Razvi, et al.
Biophysical Chemistry|December 19, 2002
Charge-charge interactions are the primary determinants of the pK values of the ionizable groups in Ribonuclease T1C Nick Pace, Beatrice M P Huyghues-Despointes, James M Briggs, et al.
Biophysical Journal|December 11, 2007
Tryptophan fluorescence reveals the presence of long-range interactions in the denatured state of ribonuclease SaRoy W Alston, Mauricio Lasagna, Gerald R Grimsley, et al.
Biophysical Journal|December 11, 2007
Peptide sequence and conformation strongly influence tryptophan fluorescenceRoy W Alston, Mauricio Lasagna, Gerald R Grimsley, et al.
Protein Science : a Publication of the Protein Society|March 4, 2010
Urea denatured state ensembles contain extensive secondary structure that is increased in hydrophobic proteinsC Nick Pace, Beatrice M P Huyghues-Despointes, Hailong Fu, et al.
Journal of Molecular Biology|March 8, 2011
Contribution of hydrophobic interactions to protein stabilityC Nick Pace, Hailong Fu, Katrina Lee Fryar, et al.
Journal of Molecular Biology|January 16, 2003
Charge-charge interactions are key determinants of the pK values of ionizable groups in ribonuclease Sa (pI=3.5) and a basic variant (pI=10.2)Douglas V Laurents, Beatrice M P Huyghues-Despointes, Marta Bruix, et al.
Protein Science : a Publication of the Protein Society|March 5, 2014
Contribution of hydrogen bonds to protein stabilityC Nick Pace, Hailong Fu, Katrina Lee Fryar, et al.
Pageof 2