ISSN:
1573-5001
Keywords:
Lyme disease
;
15N relaxation measurements
;
outer surface proteins
;
resonance assignments
;
β-sheet
;
triple resonance NMR spectroscopy
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
Notes:
Abstract The crystal structure of outer surface protein A (OspA) from Borrelia burgdorferi contains a single-layer β-sheet connecting the N- and C-terminal globular domains. The central β-sheet consists largely of polar amino acids and it is solvent-exposed on both faces, which so far appears to be unique among known protein structures. We have accomplished nearly complete backbone H, C and N and C;/Hβ assignments of OspA (28 kDa) using standard triple resonance techniques without perdeuteration. This was made possible by recording spectra at a high temperature (45 °C ). The chemical shift index and 15N T1/T2 ratios show that both the secondary structure and the global conformation of OspA in solution are similar to the crystal structure, suggesting that the unique central β-sheet is fairly rigid.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1008246908142
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