Serrano L - Search Results

1

High populations of non-native structures in the denatured state are compatible with the formation of the native folded state.

Blanco FJ, Serrano L, Forman-Kay JD. Blanco FJ, et al. Among authors: serrano l. J Mol Biol. 1998 Dec 11;284(4):1153-64. doi: 10.1006/jmbi.1998.2229. J Mol Biol. 1998. PMID: 9837733

2

The folding of an enzyme. III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure.

Serrano L, Matouschek A, Fersht AR. Serrano L, et al. J Mol Biol. 1992 Apr 5;224(3):805-18. doi: 10.1016/0022-2836(92)90563-y. J Mol Biol. 1992. PMID: 1569558 Review.

3

The folding of an enzyme. IV. Structure of an intermediate in the refolding of barnase analysed by a protein engineering procedure.

Matouschek A, Serrano L, Fersht AR. Matouschek A, et al. Among authors: serrano l. J Mol Biol. 1992 Apr 5;224(3):819-35. doi: 10.1016/0022-2836(92)90564-z. J Mol Biol. 1992. PMID: 1569559 Review.

4

The folding of an enzyme. V. H/2H exchange-nuclear magnetic resonance studies on the folding pathway of barnase: complementarity to and agreement with protein engineering studies.

Matouschek A, Serrano L, Meiering EM, Bycroft M, Fersht AR. Matouschek A, et al. Among authors: serrano l. J Mol Biol. 1992 Apr 5;224(3):837-45. doi: 10.1016/0022-2836(92)90565-2. J Mol Biol. 1992. PMID: 1569560

5

The folding of an enzyme. VI. The folding pathway of barnase: comparison with theoretical models.

Serrano L, Matouschek A, Fersht AR. Serrano L, et al. J Mol Biol. 1992 Apr 5;224(3):847-59. doi: 10.1016/0022-2836(92)90566-3. J Mol Biol. 1992. PMID: 1569561

6

Aromatic-aromatic interactions and protein stability. Investigation by double-mutant cycles.

Serrano L, Bycroft M, Fersht AR. Serrano L, et al. J Mol Biol. 1991 Mar 20;218(2):465-75. doi: 10.1016/0022-2836(91)90725-l. J Mol Biol. 1991. PMID: 2010920

7

Comparison between the phi distribution of the amino acids in the protein database and NMR data indicates that amino acids have various phi propensities in the random coil conformation.

Serrano L. Serrano L. J Mol Biol. 1995 Nov 24;254(2):322-33. doi: 10.1006/jmbi.1995.0619. J Mol Biol. 1995. PMID: 7490751

8

Analysis of i,i+5 and i,i+8 hydrophobic interactions in a helical model peptide bearing the hydrophobic staple motif.

Muñoz V, Serrano L. Muñoz V, et al. Among authors: serrano l. Biochemistry. 1995 Nov 21;34(46):15301-6. doi: 10.1021/bi00046a039. Biochemistry. 1995. PMID: 7578146

9

Folding of protein G B1 domain studied by the conformational characterization of fragments comprising its secondary structure elements.

Blanco FJ, Serrano L. Blanco FJ, et al. Among authors: serrano l. Eur J Biochem. 1995 Jun 1;230(2):634-49. doi: 10.1111/j.1432-1033.1995.tb20605.x. Eur J Biochem. 1995. PMID: 7607238 Free article.

The third peptide was previously reported to form a monomeric native beta-hairpin structure in water [Blanco, F. J., Rivas, G. & Serrano, L. (1994a) Nature Struc. Biol. 1, 584-590]. We show in this work that the beta-hairpin structure is further stabilized in 30 …

The third peptide was previously reported to form a monomeric native beta-hairpin structure in water [Blanco, F. J., Rivas, G. & Serr …

10

Side-chain interactions between sulfur-containing amino acids and phenylalanine in alpha-helices.

Viguera AR, Serrano L. Viguera AR, et al. Among authors: serrano l. Biochemistry. 1995 Jul 11;34(27):8771-9. doi: 10.1021/bi00027a028. Biochemistry. 1995. PMID: 7612617

Save citations to file

Email citations

Send citations to clipboard

Add to Collections

Add to My Bibliography

Create a file for external citation management software

Your saved search

Your RSS Feed

My NCBI Filters

Text availability

Article attribute

Article type

Publication date

908 results

Search Page