Glutamic Acid Residues of Bacteriorhodopsin at the Extracellular Surface as Determinants for Conformation and Dynamics as Revealed by Site-Directed Solid-State (13)C NMR

समान संसाधन

• Conformation and Dynamics of the [3-(13)C]Ala, [1-(13)C]Val-Labeled Truncated pharaonis Transducer, pHtrII(1–159), as Revealed by Site-Directed (13)C Solid-State NMR: Changes Due to Association with Phoborhodopsin (Sensory Rhodopsin II)
  द्वारा: Yamaguchi, Satoru, और अन्य
  प्रकाशित: (2004)
• Long-distance effects of site-directed mutations on backbone conformation in bacteriorhodopsin from solid state NMR of [1-13C]Val-labeled proteins.
  द्वारा: Tanio, M, और अन्य
  प्रकाशित: (1999)
• Primary Conformation Change in Bacteriorhodopsin on Photoexcitation
  द्वारा: Yabushita, Atsushi, और अन्य
  प्रकाशित: (2009)
• Role of Extracellular Glutamic Acids in the Stability and Energy Landscape of Bacteriorhodopsin
  द्वारा: Sapra, K. Tanuj, और अन्य
  प्रकाशित: (2008)
• Solid state NMR spectroscopy for biopolymers Principles and Applications /
  द्वारा: Saitô, Hazime., और अन्य
  प्रकाशित: (2006.)