scholarly journals 1SF08 Solid-state NMR analysis of membrane peptide and protein structures in signal transduction systems

2005 ◽  
Vol 45 (supplement) ◽  
pp. S10
Author(s):  
T. Fujiwara
Keyword(s):  
Signal Transduction ◽  
Solid State ◽  
Solid State Nmr ◽  
Protein Structures ◽  
Nmr Analysis ◽  
Membrane Peptide ◽  
Signal Transduction Systems

Protein structure by solid-state NMR spectroscopy

1987 ◽  
Vol 19 (1-2) ◽  
pp. 7-49 ◽  
Author(s):  
S. J. Opella ◽  
P. L. Stewart ◽  
K. G. Valentine
Keyword(s):  
Solid State ◽  
Nmr Spectroscopy ◽  
Solid State Nmr ◽  
Structural Information ◽  
Biological Systems ◽  
Genetic Regulation ◽  
Protein Structures ◽  
Crystalline Solid ◽  
Solid State Nmr Spectroscopy ◽  
Nmr Methods

The three-dimensional structures of proteins are among the most valuable contributions of biophysics to the understanding of biological systems (Dickerson & Geis, 1969; Creighton, 1983). Protein structures are utilized in the description and interpretation of a wide variety of biological phenomena, including genetic regulation, enzyme mechanisms, antibody recognition, cellular energetics, and macroscopic mechanical and structural properties of molecular assemblies. Virtually all of the information currently available about the structures of proteins at atomic resolution has been obtained from diffraction studies of single crystals of proteins (Wyckoff et al, 1985). However, recently developed NMR methods are capable of determining the structures of proteins and are now being applied to a variety of systems, including proteins in solution and other non-crystalline environments that are not amenable for X-ray diffraction studies. Solid-state NMR methods are useful for proteins that undergo limited overall reorientation by virtue of their being in the crystalline solid state or integral parts of supramolecular structures that do not reorient rapidly in solution. For reviews of applications of solid-state NMR spectroscopy to biological systems see Torchia and VanderHart (1979), Griffin (1981), Oldfield et al. (1982), Opella (1982), Torchia (1982), Gauesh (1984), Torchia (1984) and Opella (1986). This review describes how solid-state NMR can be used to obtain structural information about proteins. Methods applicable to samples with macroscopic orientation are emphasized.

scholarly journals Exploring Protein Structures by DNP-Enhanced Methyl Solid-State NMR Spectroscopy

2019 ◽  
Vol 141 (50) ◽  
pp. 19888-19901 ◽  
Author(s):  
Jiafei Mao ◽  
Victoria Aladin ◽  
Xinsheng Jin ◽  
Alexander J. Leeder ◽  
Lynda J. Brown ◽  
...  
Keyword(s):  
Solid State ◽  
Nmr Spectroscopy ◽  
Solid State Nmr ◽  
Protein Structures ◽  
Solid State Nmr Spectroscopy

Solid-state NMR analysis of calcium and d-mannose binding of BMY-28864, a water-soluble analogue of pradimicin A

2012 ◽  
Vol 22 (2) ◽  
pp. 1040-1043 ◽  
Author(s):  
Yu Nakagawa ◽  
Takashi Doi ◽  
K. Takegoshi ◽  
Yasuhiro Igarashi ◽  
Yukishige Ito
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Water Soluble ◽  
Nmr Analysis ◽  
Mannose Binding

Solid-state NMR analysis of steroidal conformation of 17α- and 17β-estradiol in the absence and presence of lipid environment

Steroids ◽  
2012 ◽  
Vol 77 (3) ◽  
pp. 185-192 ◽  
Author(s):  
Guo-Chian Li ◽  
Da-Rong Wang ◽  
Wenlung Chen ◽  
Der-Lii M. Tzou
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Nmr Analysis ◽  
17Β Estradiol ◽  
Lipid Environment

Crystal structure and solid-state NMR analysis of methyl 2,3,6-tri-O-acetyl-2-deoxy-2-[3-(2-phenylethyl)-ureido]-β-d-glucopyranoside

1996 ◽  
Vol 281 (1) ◽  
pp. 1-10 ◽  
Author(s):  
Roma Anulewicz ◽  
Iwona Wawer ◽  
Bogusława Piekarska-Bartoszewicz ◽  
Andrzej Temeriusz
Keyword(s):  
Crystal Structure ◽  
Solid State ◽  
Solid State Nmr ◽  
Nmr Analysis
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