Bismuto E - Search Results

1

Conformational substates of myoglobin detected by extrinsic dynamic fluorescence studies.

Bismuto E, Sirangelo I, Irace G. Bismuto E, et al. Biochemistry. 1989 Sep 19;28(19):7542-5. doi: 10.1021/bi00445a007. Biochemistry. 1989. PMID: 2611199

2

Fluorescence lifetime distribution of 1,8-anilinonaphthalenesulfonate (ANS) in reversed micelles detected by frequency domain fluorometry.

Bismuto E, Sirangelo I, Irace G. Bismuto E, et al. Biophys Chem. 1992 Sep;44(2):83-90. doi: 10.1016/0301-4622(92)85040-b. Biophys Chem. 1992. PMID: 1391609

3

Salt-induced refolding of myoglobin at acidic pH: molecular properties of a partly folded intermediate.

Bismuto E, Sirangelo I, Irace G. Bismuto E, et al. Arch Biochem Biophys. 1992 Nov 1;298(2):624-9. doi: 10.1016/0003-9861(92)90458-9. Arch Biochem Biophys. 1992. PMID: 1416991

4

Molecular organization and dynamics of the outer membrane of Salmonella thyphimurium mutant strains detected by frequency domain fluorometry.

Bismuto E, Sirangelo I, Adinolfi A, Galdiero F, Tufano MA, Sommese L, Irace G. Bismuto E, et al. Arch Biochem Biophys. 1991 May 1;286(2):518-23. doi: 10.1016/0003-9861(91)90074-s. Arch Biochem Biophys. 1991. PMID: 1897974

5

Conformational dynamics of unfolded peptides as a function of chain length: a frequency domain fluorescence approach.

Bismuto E, Sirangelo I, Irace G. Bismuto E, et al. Arch Biochem Biophys. 1991 Nov 15;291(1):38-42. doi: 10.1016/0003-9861(91)90102-o. Arch Biochem Biophys. 1991. PMID: 1929433

6

Multiple conformational states in myoglobin revealed by frequency domain fluorometry.

Bismuto E, Irace G, Gratton E. Bismuto E, et al. Biochemistry. 1989 Feb 21;28(4):1508-12. doi: 10.1021/bi00430a013. Biochemistry. 1989. PMID: 2719914

7

Effect of unfolding on the tryptophanyl fluorescence lifetime distribution in apomyoglobin.

Bismuto E, Gratton E, Irace G. Bismuto E, et al. Biochemistry. 1988 Mar 22;27(6):2132-6. doi: 10.1021/bi00406a047. Biochemistry. 1988. PMID: 3378049

8

Unfolding pathway of myoglobin: effect of denaturants on solvent accessibility to tyrosyl residues detected by second-derivative spectroscopy.

Ragone R, Colonna G, Bismuto E, Irace G. Ragone R, et al. Among authors: bismuto e. Biochemistry. 1987 Apr 21;26(8):2130-4. doi: 10.1021/bi00382a010. Biochemistry. 1987. PMID: 3620442

9

Unfolding pathway of myoglobin. Evidence for a multistate process.

Bismuto E, Colonna G, Irace G. Bismuto E, et al. Biochemistry. 1983 Aug 30;22(18):4165-70. doi: 10.1021/bi00287a001. Biochemistry. 1983. PMID: 6626499

The free energy of unfolding of horse myoglobin has been calculated from the denaturation pattern induced by guanidine hydrochloride as well as by acid. The delta GH2O, i.e., the value in the absence of denaturant obtained by using the two-state transition model, was found …

The free energy of unfolding of horse myoglobin has been calculated from the denaturation pattern induced by guanidine hydrochloride as well …

10

Structure and dynamics of the acidic compact state of apomyoglobin by frequency-domain fluorometry.

Bismuto E, Gratton E, Sirangelo I, Irace G. Bismuto E, et al. Eur J Biochem. 1993 Nov 15;218(1):213-9. doi: 10.1111/j.1432-1033.1993.tb18367.x. Eur J Biochem. 1993. PMID: 8243466 Free article.

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