NMR of fd coat protein

✍ Scribed by Cross, T. A. ;Opella, S. J.

• Book ID: 102440219
• Publisher: Wiley (John Wiley & Sons)
• Year: 1979
• Tongue: English
• Weight: 400 KB
• Volume: 11
• Category: Article
• ISSN: 0091-7419
• DOI: 10.1002/jss.400110204

✦ Synopsis

Abstract

The conformations of the major coat protein of a filamentous bacteriophage can be described by nuclear magnetic resonance spectroscopy of the protein and the virus. The NMR experiments involve detection of the ^13^C and ^1^H nuclei of the coat protein. Both the ^13^C and ^1^H nuclear magnetic resonance (NMR) spectra show that regions of the polypeptide chain have substantially more motion than a typical globular protein. The fd coat protein was purified by gel chromatography of the SDS solubilized virus. Natural abundance ^13^C NMR spectra at 38 MHz resolve all of the nonprotonated aromatic carbons from the three phenylalanines, two tyrosines, and one tryptophan of the coat protein. The α carbons of the coat protein show at least two different classes of relaxation behavior, indicative of substantial variation in the motion of the backbone carbons in contrast to the rigidity of the α carbons of globular proteins. The ^1^H spectrum at 360 MHz shows all of the aromatic carbons and many of the amide protons. Titration of a ^1^H spectra gives the pKas for the tyrosines.