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Proteins|July 24, 2009
Increasing protein stability by improving beta-turnsHailong Fu, Gerald R Grimsley, Abbas Razvi, et al.
Pacific Symposium on Biocomputing. Pacific Symposium on Biocomputing|February 27, 2003
A path planning-based study of protein folding with a case study of hairpin formation in protein G and LGuang Song, Shawna Thomas, Ken A Dill, 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.
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|September 21, 2004
Contribution of single tryptophan residues to the fluorescence and stability of ribonuclease SaRoy W Alston, Lubica Urbanikova, Jozef Sevcik, 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.
The Journal of Physical Chemistry. B|March 29, 2007
Single-molecule electrophoresis of beta-hairpin peptides by electrical recordings and Langevin dynamics simulationsCarl P Goodrich, Serdal Kirmizialtin, Beatrice M Huyghues-Despointes, et al.
Journal of the American Chemical Society|November 19, 2009
Hydrogen bonding of beta-turn structure is stabilized in D(2)OYounhee Cho, Laura B Sagle, Satoshi Iimura, et al.
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