Fersht AR - Search Results

1

An N-terminal fragment of barnase has residual helical structure similar to that in a refolding intermediate.

Sancho J, Neira JL, Fersht AR. Sancho J, et al. Among authors: fersht ar. J Mol Biol. 1992 Apr 5;224(3):749-58. doi: 10.1016/0022-2836(92)90559-3. J Mol Biol. 1992. PMID: 1569554

2

Search for nucleation sites in smaller fragments of chymotrypsin inhibitor 2.

Itzhaki LS, Neira JL, Ruiz-Sanz J, de Prat Gay G, Fersht AR. Itzhaki LS, et al. Among authors: fersht ar. J Mol Biol. 1995 Nov 24;254(2):289-304. doi: 10.1006/jmbi.1995.0617. J Mol Biol. 1995. PMID: 7490749

3

Conformational pathway of the polypeptide chain of chymotrypsin inhibitor-2 growing from its N terminus in vitro. Parallels with the protein folding pathway.

de Prat Gay G, Ruiz-Sanz J, Neira JL, Corrales FJ, Otzen DE, Ladurner AG, Fersht AR. de Prat Gay G, et al. Among authors: fersht ar. J Mol Biol. 1995 Dec 15;254(5):968-79. doi: 10.1006/jmbi.1995.0669. J Mol Biol. 1995. PMID: 7500364

4

Folding of a nascent polypeptide chain in vitro: cooperative formation of structure in a protein module.

De Prat Gay G, Ruiz-Sanz J, Neira JL, Itzhaki LS, Fersht AR. De Prat Gay G, et al. Among authors: fersht ar. Proc Natl Acad Sci U S A. 1995 Apr 25;92(9):3683-6. doi: 10.1073/pnas.92.9.3683. Proc Natl Acad Sci U S A. 1995. PMID: 7731965 Free PMC article.

5

Folding of barnase in parts.

Kippen AD, Sancho J, Fersht AR. Kippen AD, et al. Among authors: fersht ar. Biochemistry. 1994 Mar 29;33(12):3778-86. doi: 10.1021/bi00178a039. Biochemistry. 1994. PMID: 8142379

6

Long-range surface charge-charge interactions in proteins. Comparison of experimental results with calculations from a theoretical method.

Loewenthal R, Sancho J, Reinikainen T, Fersht AR. Loewenthal R, et al. Among authors: fersht ar. J Mol Biol. 1993 Jul 20;232(2):574-83. doi: 10.1006/jmbi.1993.1412. J Mol Biol. 1993. PMID: 8345524

7

Circular dichroism studies of barnase and its mutants: characterization of the contribution of aromatic side chains.

Vuilleumier S, Sancho J, Loewenthal R, Fersht AR. Vuilleumier S, et al. Among authors: fersht ar. Biochemistry. 1993 Oct 5;32(39):10303-13. doi: 10.1021/bi00090a005. Biochemistry. 1993. PMID: 8399173

8

The folding pathway of a protein at high resolution from microseconds to seconds.

Nölting B, Golbik R, Neira JL, Soler-Gonzalez AS, Schreiber G, Fersht AR. Nölting B, et al. Among authors: fersht ar. Proc Natl Acad Sci U S A. 1997 Feb 4;94(3):826-30. doi: 10.1073/pnas.94.3.826. Proc Natl Acad Sci U S A. 1997. PMID: 9023341 Free PMC article.

9

An NMR study on the beta-hairpin region of barnase.

Neira JL, Fersht AR. Neira JL, et al. Among authors: fersht ar. Fold Des. 1996;1(3):231-41. doi: 10.1016/s1359-0278(96)00034-x. Fold Des. 1996. PMID: 9079384

10

Following co-operative formation of secondary and tertiary structure in a single protein module.

Neira JL, Itzhaki LS, Ladurner AG, Davis B, de Prat Gay G, Fersht AR. Neira JL, et al. Among authors: fersht ar. J Mol Biol. 1997 Apr 25;268(1):185-97. doi: 10.1006/jmbi.1997.0932. J Mol Biol. 1997. PMID: 9149151

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