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Protein Science : a Publication of the Protein Society|August 10, 2000
Charge-charge interactions influence the denatured state ensemble and contribute to protein stabilityC N Pace, R W Alston, K L ShawBiochemistry|June 22, 1993
Investigation of ribonuclease T1 folding intermediates by hydrogen-deuterium amide exchange-two-dimensional NMR spectroscopyL S Mullins, C N Pace, F M RaushelBiochemistry|March 17, 1992
Urea denaturation of barnase: pH dependence and characterization of the unfolded stateC N Pace, D V Laurents, R E EricksonAmerican Family Physician|November 1, 1991
GnRH agonists: gonadorelin, leuprolide and nafarelinJ N Pace, J L Miller, L I RoseJournal of Counseling Psychology|April 10, 2025
I kotturå-ta, I minetgot-ta: A qualitative investigation of mental health perceptions and cultural strengths among CHamoru peopleShawntell N Pace, Tabitha Meng Rominger, Collette Chapman-HilliardBiochemistry|March 13, 1990
pH dependence of the urea and guanidine hydrochloride denaturation of ribonuclease A and ribonuclease T1C N Pace, D V Laurents, J A ThomsonProceedings of the National Academy of Sciences of the United States of America|April 1, 1997
A direct comparison of helix propensity in proteins and peptidesJ K Myers, C N Pace, J M ScholtzActa Biologica Et Medica Germanica|January 1, 1981
Globular protein stability: aspects of interest in protein turnoverC N Pace, L M Fisher, J F CupoProtein Science : a Publication of the Protein Society|July 1, 1997
Conformational stability of ribonuclease T1 determined by hydrogen-deuterium exchangeL S Mullins, C N Pace, F M RaushelBiochemistry|September 9, 1997
Helix propensities are identical in proteins and peptidesJ K Myers, C N Pace, J M ScholtzPageof 10