Sentence examples for secondary sheets from inspiring English sources

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If more than one sheet was required for a county, the county name would be amended on secondary sheets to indicate the order the sheets were in.

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In summary, FTIR spectroscopy of S-MB and MB in lipids and lipid-mimics showed that these peptides exhibit similar conformations, with primary α-helix and secondary β-sheet and loop-turns.

FTIR spectra of Mini-B and Super Mini-B in either lipids or lipid-mimics indicated that these peptides share similar conformations, with primary α-helix and secondary β-sheet and loop-turns.

Yeast prions form amyloid deposits characterized by a secondary beta-sheet structure and stain positive for amyloid dyes.

Multiple crystal averaging across four distinct data sets (KAu CN 2, DMA, Au(NO3 4 and native, using the program DMMULTI (Cowtan and Main, 1993; Winn et al., 2011), revealed the domain swap in the secondary β-sheet portion of the SH2 domain.

FT-IR and DSC evidences suggest that the β-alanine trimer segments in both 3a and 3b exist exclusively in the β-sheet secondary structure, and the β-sheets stack to form crystals in the continuous SBR phase.

Availability: http://www.csse.monash.edu.au/~karun/sst Contact: [email protected] (or [email protected]) Periodic hydrogen-bonding patterns in globular proteins give rise to elements of secondary structure helices and sheets.

The lack of these distance restraints prevented the generation of a well-converged solution structure; however, in support of the CD and FTIR spectroscopic data, the NMR data are consistent with α-sheet secondary structure and inconsistent with α-helix, random coil, and β-sheet structures.

The high β-sheet content suggested that the Rv0045c protein possessed abundant β-sheet secondary structures, which is in accordance with the α/β-hydrolase fold [15] and implied that the Rv0045c protein may fall into the description of the α/β-hydrolase fold by Nardini and colleagues [16].

Data from CD spectroscopy analysis showed that the Rv0045c protein is rich in β-sheet secondary structure, indicating that the enzyme should possess a very stable and substantial β-sheet core which helps to stabilize the architecture of the enzyme, thus ensuring that the pathogen can survive in strong environments.

In many cases, the intrinsic complexity of the β-sheet secondary structure requires the combination of these approaches to ensure appropriate stabilization of the β-sheet.

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