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1

Spektroskopia magnetycznego rezonansu jądrowego w wyznaczaniu budowy białek

100%

Ejchart A.

Kosmos

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2004

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vol. 53

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issue 3-4

263-270

EN

Summary Nuclear magnetic resonance spectroscopy (NMR) is a method well suited to play an important part in proteomics programs. It provides structural information at the atomic resolution. Isotopes of biologically important elements, 1H, 13C, 15N, and 31P, display narrow resonance lines while the most abundant nitrogen (14N) and carbon (12C) isotopes are uselessness in the NMR studies of macromolecules. Internuclear interactions, modulated by even small structural and conformational changes, influence line shape and intensity of signals in NMR spectra. Last but not least, NMR provides high resolution structures in solution allowing to study those proteins that fail to crystallize or to compare differences between their crystal and solution structures. The pros and cons of NMR spectroscopy as a tool for the protein structure determination are discussed. Recently, the advance in the NMR equipment, spectral techniques and isotope labelling resulted in an enormous growth of the number of NMR-determined protein structures. Modern NMR-based procedure of structure determination comprises three stages: assignment of as many signals as possible in the spectra of NMR-active isotopes, identification of structural constraints, and calculation of a family of three-dimensional structures fulfilling experimental constraints. Approaches used at the first two stages depend on the size of the protein studied whereas the approach applied at the third stage depends on the type and number of identified constraints.

2

15N magnetic relaxation study of backbone dynamics of the ribosome-associated cold shock response protein Yfia of Escherichia coli

51%

Zhukov I., Bayer P., Schölermann B., Ejchart A.

Acta Biochimica Polonica

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2007

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vol. 54

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issue 4

769-775

EN

In the solution structure of the ribosome-associated cold shock response protein Yfia of Escherichia coli in the free state two structural segments can be distinguished: a well structured, rigid N-terminal part displaying a βαβββα topology and a flexible C-terminal tail comprising last 20 amino-acid residues. The backbone dynamics of Yfia protein was studied by 15N nuclear magnetic relaxation at three magnetic fields and analyzed using model-free approach. The overall diffusional tumbling of the N-terminal part is strongly anisotropic with a number of short stretches showing increased mobility either on a subnanosecond time scale, or a micro- to millisecond time scale, or both. In contrast, the unstructured polypeptide chain of the C-terminal part, which cannot be regarded as a rigid structure, shows the predominance of fast local motions over slower ones, both becoming faster closer to the C-terminus.

3

NMR measurements of proton exchange between solvent and peptides and proteins

45%

Wójcik J., Ruszczyńska K., Zhukov I., Ejchart A.

Acta Biochimica Polonica

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1999

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vol. 46

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issue 3

651-663

4

Factors improving the accuracy of determination of 15N relaxation parameters in proteins

45%

Zhukov I., Ejchart A.

Acta Biochimica Polonica

|

1999

|

vol. 46

|

issue 3

665-671

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1 Schölermann B.

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Spektroskopia magnetycznego rezonansu jądrowego w wyznaczaniu budowy białek

15N magnetic relaxation study of backbone dynamics of the ribosome-associated cold shock response protein Yfia of Escherichia coli

NMR measurements of proton exchange between solvent and peptides and proteins

Factors improving the accuracy of determination of 15N relaxation parameters in proteins