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Items: 8

1.

Coupling between trans/cis proline isomerization and protein stability in staphylococcal nuclease.

Truckses DM, Somoza JR, Prehoda KE, Miller SC, Markley JL.

Protein Sci. 1996 Sep;5(9):1907-16.

2.

Quantitative interpretations of double mutations of enzymes.

Mildvan AS, Weber DJ, Kuliopulos A.

Arch Biochem Biophys. 1992 May 1;294(2):327-40. Review. Erratum in: Arch Biochem Biophys 1992 Aug 15;297(1):18.

PMID:
1567189
3.

γ-(S)-Trifluoromethyl proline: evaluation as a structural substitute of proline for solid state (19)F-NMR peptide studies.

Kubyshkin V, Afonin S, Kara S, Budisa N, Mykhailiuk PK, Ulrich AS.

Org Biomol Chem. 2015 Mar 21;13(11):3171-3181. doi: 10.1039/c5ob00034c. Review.

PMID:
25703116
4.

Staphylococcal nuclease reviewed: a prototypic study in contemporary enzymology. IV. The nuclease as a model for protein folding.

Tucker PW, Hazen EE Jr, Cotton FA.

Mol Cell Biochem. 1979 Feb 9;23(3):131-41. Review.

PMID:
90333
5.

An evaluation of peptide-bond isosteres.

Choudhary A, Raines RT.

Chembiochem. 2011 Aug 16;12(12):1801-7. doi: 10.1002/cbic.201100272. Epub 2011 Jul 12. Review.

6.

[Staphylococcal nuclease: a model system for the study of protein conformation and function].

Anfinsen CB.

Seikagaku. 1972 Jul;44(7):279-86. Review. Japanese. No abstract available.

PMID:
4565280
7.

Stability and self-organization of proteins.

Jaenicke R.

Naturwissenschaften. 1988 Dec;75(12):604-10. Review.

PMID:
3070391
8.

Structural consequences of mutation.

Eigenbrot C, Kossiakoff AA.

Curr Opin Biotechnol. 1992 Aug;3(4):333-7. Review.

PMID:
1368433

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