BIOFISICA Y BIOTECNOLOGIA MOLECULAR
BIOFISICA Y BIOTECNOLOGIA MOLE
University of Cambridge
Cambridge, Reino UnidoPublicaciones en colaboración con investigadores/as de University of Cambridge (10)
2016
2003
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Characterization of single-tryptophan mutants of histidine-containing phosphocarrier protein: Evidence for local rearrangements during folding from high concentrations of denaturant
Biochemistry, Vol. 42, Núm. 17, pp. 4883-4895
1995
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A Calorimetric Study of the Thermal Stability of Barstar and its Interaction with Barnase
Biochemistry, Vol. 34, Núm. 15, pp. 5224-5233
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Conformational pathway of the polypeptide chain of chymotrypsin inhibitor-2 growing from its N terminus in vitro. Parallels with the protein folding pathway
Journal of Molecular Biology, Vol. 254, Núm. 5, pp. 968-979
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Folding of a nascent polypeptide chain in vitro: Cooperative formation of structure in a protein module
Proceedings of the National Academy of Sciences of the United States of America, Vol. 92, Núm. 9, pp. 3683-3686
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Protein Fragments as Models for Events in Protein Folding Pathways: Protein Engineering Analysis of the Association of Two Complementary Fragments of the Barley Chymotrypsin Inhibitor 2 (CI-2)
Biochemistry, Vol. 34, Núm. 5, pp. 1695-1701
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Search for nucleation sites in smaller fragments of chymotrypsin inhibitor 2
Journal of Molecular Biology, Vol. 254, Núm. 2, pp. 289-304
1994
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A Calorimetric Study of the Thermal Stability of Barnase and Its Interaction with 3′GMP
Biochemistry, Vol. 33, Núm. 13, pp. 3919-3926
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Generation of a Family of Protein Fragments for Structure-Folding Studies. 2. Kinetics of Association of the Two Chymotrypsin Inhibitor-2 Fragments
Biochemistry, Vol. 33, Núm. 25, pp. 7964-7970
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The structure of the transition state for the association of two fragments of the barley chymotrypsin inhibitor 2 to generate native-like protein: Implications for mechanisms of protein folding
Proceedings of the National Academy of Sciences of the United States of America, Vol. 91, Núm. 23, pp. 10943-10946