We've updated our Privacy Policy to make it clearer how we use your personal data.

We use cookies to provide you with a better experience. You can read our Cookie Policy here.

Advertisement
Resolving Nitrogen-15 and Proton Chemical Shifts for the Mobile Segments of Elastin with Two-Dimensional NMR Spectroscopy
News

Resolving Nitrogen-15 and Proton Chemical Shifts for the Mobile Segments of Elastin with Two-Dimensional NMR Spectroscopy

Resolving Nitrogen-15 and Proton Chemical Shifts for the Mobile Segments of Elastin with Two-Dimensional NMR Spectroscopy
News

Resolving Nitrogen-15 and Proton Chemical Shifts for the Mobile Segments of Elastin with Two-Dimensional NMR Spectroscopy

Read time:
 

Want a FREE PDF version of This News Story?

Complete the form below and we will email you a PDF version of "Resolving Nitrogen-15 and Proton Chemical Shifts for the Mobile Segments of Elastin with Two-Dimensional NMR Spectroscopy"

First Name*
Last Name*
Email Address*
Country*
Company Type*
Job Function*
Would you like to receive further email communication from Technology Networks?

Technology Networks Ltd. needs the contact information you provide to us to contact you about our products and services. You may unsubscribe from these communications at any time. For information on how to unsubscribe, as well as our privacy practices and commitment to protecting your privacy, check out our Privacy Policy

Hydrated elastin is characterized by large segments that undergo “liquidlike” motions that limit the efficiency of cross-polarization. The refocused INEPT experiment is used to target these extensive, mobile regions of this protein. Numerous peaks are detected in the backbone amide region of the protein, and their chemical shifts indicate the completely unstructured, “random coil” model for elastin is unlikely. Instead, more evidence is gathered that supports a characteristic ensemble of conformations in this rubberlike protein.

The full article is published online in The Journal of Biological Chemistry and is free to access.

Advertisement