Sirangelo I - Search Results

1

Role of tryptophanyl residues in driving myoglobin folding.

Sirangelo I, Casillo M, Malmo C, Irace G. Sirangelo I, et al. Boll Soc Ital Biol Sper. 2001 Jan-Mar;77(1-3):1-6. Boll Soc Ital Biol Sper. 2001. PMID: 11512493

2

Tryptophanyl substitutions in apomyoglobin determine protein aggregation and amyloid-like fibril formation at physiological pH.

Sirangelo I, Malmo C, Casillo M, Mezzogiorno A, Papa M, Irace G. Sirangelo I, et al. J Biol Chem. 2002 Nov 29;277(48):45887-91. doi: 10.1074/jbc.M207659200. Epub 2002 Sep 19. J Biol Chem. 2002. PMID: 12244112 Free article.

3

Resolution of tryptophan-ANS fluorescence energy transfer in apomyoglobin by site-directed mutagenesis.

Sirangelo I, Malmo C, Casillo M, Irace G. Sirangelo I, et al. Photochem Photobiol. 2002 Oct;76(4):381-4. doi: 10.1562/0031-8655(2002)076<0381:rotafe>2.0.co;2. Photochem Photobiol. 2002. PMID: 12405143

4

Tryptophanyl substitutions in apomyoglobin affect conformation and dynamic properties of AGH subdomain.

Sirangelo I, Iannuzzi C, Malmo C, Irace G. Sirangelo I, et al. Biopolymers. 2003 Dec;70(4):649-54. doi: 10.1002/bip.10503. Biopolymers. 2003. PMID: 14648775

5

Resolution of the individual tryptophanyl contributions to the near-ultraviolet dichroic activity of apomyoglobin.

Sirangelo I, Irace G, Bismuto E. Sirangelo I, et al. Photochem Photobiol. 1994 Jun;59(6):611-4. doi: 10.1111/j.1751-1097.1994.tb09664.x. Photochem Photobiol. 1994. PMID: 8066120

6

Apomyoglobin folding intermediates characterized by the hydrophobic fluorescent probe 8-anilino-1-naphthalene sulfonate.

Sirangelo I, Bismuto E, Tavassi S, Irace G. Sirangelo I, et al. Biochim Biophys Acta. 1998 Jun 11;1385(1):69-77. doi: 10.1016/s0167-4838(98)00038-7. Biochim Biophys Acta. 1998. PMID: 9630524

7

Tryptophanyl contributions to apomyoglobin fluorescence resolved by site-directed mutagenesis.

Sirangelo I, Tavassi S, Irace G. Sirangelo I, et al. Biochim Biophys Acta. 2000 Feb 9;1476(2):173-80. doi: 10.1016/s0167-4838(99)00257-5. Biochim Biophys Acta. 2000. PMID: 10669783

8

The effect of tryptophanyl substitution on folding and structure of myoglobin.

Sirangelo I, Tavassi S, Martelli PL, Casadio R, Irace G. Sirangelo I, et al. Eur J Biochem. 2000 Jul;267(13):3937-45. doi: 10.1046/j.1432-1327.2000.01401.x. Eur J Biochem. 2000. PMID: 10866792 Free article.

9

Single tryptophanyl substitutions affect the structure of apomyoglobin.

Sirangelo I, Tavassi S, Irace G. Sirangelo I, et al. Boll Soc Ital Biol Sper. 1998 Sep-Oct;74(9-10):83-9. Boll Soc Ital Biol Sper. 1998. PMID: 10904557

10

Hexafluoroisopropanol and acid destabilized forms of apomyoglobin exhibit structural differences.

Sirangelo I, Dal Piaz F, Malmo C, Casillo M, Birolo L, Pucci P, Marino G, Irace G. Sirangelo I, et al. Biochemistry. 2003 Jan 21;42(2):312-9. doi: 10.1021/bi020447f. Biochemistry. 2003. PMID: 12525158 Free article.

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