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Folding & Design|January 1, 1997
Favourable native-like helical local interactions can accelerate protein foldingA R Viguera, V Villegas, F X Avilés, et al.Journal of Molecular Biology|January 26, 1996
Conformational analysis of peptides corresponding to beta-hairpins and a beta-sheet that represent the entire sequence of the alpha-spectrin SH3 domainA R Viguera, M A Jiménez, M Rico, et al.Biochemistry|September 13, 1994
Characterization of the interaction of natural proline-rich peptides with five different SH3 domainsA R Viguera, J L Arrondo, A Musacchio, et al.Protein Engineering|December 1, 1994
Molecular modeling of the interaction of polyproline-based peptides with the Abl-SH3 domain: rational modification of the interactionM T Pisabarro, A R Ortiz, A R Viguera, et al.Biophysical Chemistry|May 18, 1999
A thermodynamic analysis of a family of small globular proteins: SH3 domainsV V Filimonov, A I Azuaga, A R Viguera, et al.Biochemistry|March 1, 1994
Thermodynamic and kinetic analysis of the SH3 domain of spectrin shows a two-state folding transitionA R Viguera, J C Martínez, V V Filimonov, et al.Biochemistry|January 15, 1999
Thermodynamic analysis of alpha-spectrin SH3 and two of its circular permutants with different loop lengths: discerning the reasons for rapid folding in proteinsJ C Martínez, A R Viguera, R Berisio, et al.European Journal of Biochemistry|December 15, 1992
The uncoupling protein from brown adipose tissue mitochondria. The environment of the tryptophan residues as revealed by quenching of the intrinsic fluorescenceA R Viguera, F M Goñi, E RialBiochemistry|April 13, 1993
Time-resolved and equilibrium measurements of the effects of poly(ethylene glycol) on small unilamellar phospholipid vesiclesA R Viguera, M Mencía, F M GoñiThe Journal of Biological Chemistry|February 15, 1990
A water-soluble polylysine-retinaldehyde Schiff base. Stability in aqueous and nonaqueous environmentsA R Viguera, M J Villa, F M GoñiPageof 56