Studying natural structural protein fibers by solid-state nuclear magnetic resonance

✍ Scribed by Alexandre A. Arnold; Isabelle Marcotte

• Publisher: John Wiley and Sons
• Year: 2009
• Tongue: English
• Weight: 603 KB
• Volume: 34A
• Category: Article
• ISSN: 1546-6086
• DOI: 10.1002/cmr.a.20132

✦ Synopsis

Abstract

As a consequence of evolutionary pressure, various organisms have developed structural fibers displaying a range of exceptional mechanical properties adapted specifically to their functions. An understanding of these properties at the molecular level requires a detailed description of local structure, orientation with respect to the fiber and size of constitutive units, and dynamics on various timescales. The size and lack of long‐range order in these protein systems constitute an important challenge to classical structural techniques such as high‐resolution NMR and X‐ray diffraction. Solid‐state NMR overcomes these constraints and is uniquely suited to the study of these inherently disordered systems. Solid‐state NMR experiments developed or applied to determine structure, orientation, and dynamics of these complex proteins will be reviewed and illustrated through examples of their applications to fibers such as spider and silkworm silks, collagen, elastin, and keratin. © 2009 Wiley Periodicals, Inc. Concepts Magn Reson Part A 34A: 24–27, 2009.