Protein nanocrystallography: a new approach to structural proteomics

Pechkova, Eugenia; Nicolini, Claudio

doi:10.1016/j.tibtech.2004.01.011

Cited by 62 publications

(83 citation statements)

References 45 publications

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“…Raman Spectroscopy peak assignment is based on [35], namely lysozyme molecule has 6 Trp residues. Trp123 is located closely to C-end of the lysozyme.…”

Section: Resultsmentioning

confidence: 99%

“…We suppose that difference between LB and classical crystals and changes observed for larger lysozyme LB crystals and for LB crystals with different time after nucleation occur near the C-end of lysozyme, since this region is the most sensitive to any environmental changes [35]. We suggest in Figure 7 that LB crystal growing with time is accompanied by:…”

Section: I8s 4iatmentioning

confidence: 92%

“…formation of S-S bonds resulting in the decrease of amount of SH-bonds in Cys residues. This is manifested in Raman Spectra as the increase in relative intensity of peak at 505 cm-1 and the decrease in peak intensity at 634 cm -1 [35]. The relative inputs of Raman Spectra peaks at 760, 1001 and 1010 cm -1 into the spectrum (ratios of intensities I760/I865, I1010/I865 and I1010/I865) increase with time and corresponds to the increased manifestation of vibrations of indole ring, ring breathing of Trp and of ring breathing of Phe.…”

Section: I8s 4iatmentioning

confidence: 99%

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In situ Monitoring By Raman Spectroscopy of Lysozyme Conformation during “Nanotemplate” Induced Crystallization

Nicolini

Belmonte²,

Максимов³

et al. 2013

J Microb Biochem Technol

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Using Raman spectroscopy and lysozyme, this latter as model protein, we investigate the differences in protein conformation before and after LB nanotemplate-induced crystal nucleation and growth. It was found that the main difference in lysozyme conformation is associated to the higher amount of S-S bonds in lysozyme of LB crystals, probably in C-end of protein, resulting in the higher stiffness of the lysozyme molecules and LB crystal in a whole. Growth in size of LB crystal over time is also accompanied by the formation of S-S bonds. Atomic structure, determined by X-ray diffraction, correlates Raman spectroscopy results confirm the main differences between LB and classical crystals are in terms of water molecules environment previously associated to the increased radiation stability of LB crystals.

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“…Raman Spectroscopy peak assignment is based on [35], namely lysozyme molecule has 6 Trp residues. Trp123 is located closely to C-end of the lysozyme.…”

Section: Resultsmentioning

confidence: 99%

Section: I8s 4iatmentioning

confidence: 92%

Section: I8s 4iatmentioning

confidence: 99%

See 1 more Smart Citation

In situ Monitoring By Raman Spectroscopy of Lysozyme Conformation during “Nanotemplate” Induced Crystallization

Nicolini

Belmonte²,

Максимов³

et al. 2013

J Microb Biochem Technol

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show abstract

“…Different crystallization techniques have been proposed over the past decades, such as the classical vapor hanging drop method, its variant the sitting drop method, dialysis, cryotemperature, gel, batch, and the innovative microgravity (space) techniques like free interface diffusion (FID) and counter-ion diffusion (CID). LangmuirBlodgett (LB)-based crystallization approach [1][2][3] has been shown to represent a valid alternative for fast crystallizing proteins which are difficult to obtain with other techniques [4][5][6].…”

Section: Introductionmentioning

confidence: 99%

Langmuir-Blodgett Technology for Drugs Production and Delivery: Insights and Implications from an In Silico Study

Bragazzi¹,

Pechkova²,

Nicolini³

2017

NanoWorld J

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Insulin dynameomics here reported as a database pertaining to a series of Molecular Dynamics (MD) ran for Protein Data Bank (PDB) entries consisting in bioinformatics and molecular dynamics simulation of Langmuir-Blodgett and classical insulin with and without insulin receptor, appears to have profound implications for drug design and endocrinology. The slight differences in conformation and dynamics here reported may indeed explain why LB-insulin is more stable when binds to its receptor (lower free energy) and this could be useful when designing new drugs and pharmaceuticals.

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“…Protein crystal nucleation and growth are facilitated and enhanced through a Langmuir-Blodgett (LB)-based nanobiotemplate [8][9][10][11][12][13][14].…”

Section: Introductionmentioning

confidence: 99%

Ab Initio Semi-Quantitative Analysis of Micro-Beam Grazing-Incidence Small-Angle X-Ray Scattering (Μ-GISAXS) during Protein Crystal Nucleation and Growth

Nicolini¹,

Bragazzi²,

Pechkova³

et al. 2014

J Proteomics Bioinform

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Protein nanocrystallography: a new approach to structural proteomics

Cited by 62 publications

References 45 publications

In situ Monitoring By Raman Spectroscopy of Lysozyme Conformation during “Nanotemplate” Induced Crystallization

In situ Monitoring By Raman Spectroscopy of Lysozyme Conformation during “Nanotemplate” Induced Crystallization

Langmuir-Blodgett Technology for Drugs Production and Delivery: Insights and Implications from an In Silico Study

Ab Initio Semi-Quantitative Analysis of Micro-Beam Grazing-Incidence Small-Angle X-Ray Scattering (Μ-GISAXS) during Protein Crystal Nucleation and Growth

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