scholarly journals Osmolyte-Induced Perturbations of Hydrogen Bonding between Hydration Layer Waters: Correlation with Protein Conformational Changes

2009 ◽  
Vol 113 (52) ◽  
pp. 16632-16642 ◽  
Author(s):  
Feng Guo ◽  
Joel M. Friedman
Keyword(s):  
Hydrogen Bonding ◽  
Conformational Changes ◽  
Hydration Layer ◽  
Protein Conformational Changes

scholarly journals Hydrogen bonding changes of internal water molecules in rhodopsin during metarhodopsin I and metarhodopsin II formation

1998 ◽  
Vol 329 (3) ◽  
pp. 713-717 ◽  
Author(s):  
Parshuram RATH ◽  
Frank DELANGE ◽  
J. Willem DEGRIP ◽  
J. Kenneth ROTHSCHILD
Keyword(s):  
Hydrogen Bonding ◽  
Conformational Changes ◽  
Structural Changes ◽  
Integral Membrane Protein ◽  
Water Molecules ◽  
Rod Outer Segments ◽  
Oh Groups ◽  
Protein Conformational Changes ◽  
Hydrogen Deuterium ◽  
Fourier Transform Ir

Rhodopsin is a 7-helix, integral membrane protein found in the rod outer segments, which serves as the light receptor in vision. Light absorption by the retinylidene chromophore of rhodopsin triggers an 11-cis → all-trans isomerization, followed by a series of protein conformational changes, which culminate in the binding and activation of the G-protein transducin by the metarhodopsin II (Meta II) intermediate. Fourier transform IR difference spectroscopy has been used to investigate the structural changes that water, as well as other OH- and NH-containing groups, undergo during the formation of the metarhodopsin I (Meta I) and Meta II intermediates. Bands associated with the OH stretch modes of water are identified by characteristic downshifts upon substitution of H218O for H2O. Compared with earlier work, several negative bands associated with water molecules in unphotolysed rhodopsin were detected, which shift to lower frequencies upon formation of the Meta I and Meta II intermediates. These data indicate that at least one water molecule undergoes an increase in hydrogen bonding upon formation of the Meta I intermediate, while at least one other increases its hydrogen bonding during Meta II formation. Amino acid residue Asp-83, which undergoes a change in its hydrogen bonding during Meta II formation, does not appear to interact with any of the structurally active water molecules. Several NH and/or OH groups, which are inaccessible to hydrogen/deuterium exchange, also undergo alterations during Meta I and Meta II formation.

scholarly journals Protein conformational changes and myelin solubilization by anion-detergent solutions

FEBS Letters ◽  
1992 ◽  
Vol 309 (3) ◽  
pp. 376-380 ◽  
Author(s):  
Jaime Monreal ◽  
Pedro Carmona ◽  
Pilar Regueiro ◽  
Ricardo S. Diaz
Keyword(s):  
Conformational Changes ◽  
Protein Conformational Changes ◽  
Detergent Solutions

Protein conformational changes revealed by optical spectroscopic reflectometry in porous silicon multilayers

2008 ◽  
Vol 21 (3) ◽  
pp. 035115 ◽  
Author(s):  
Edoardo De Tommasi ◽  
Ilaria Rea ◽  
Ivo Rendina ◽  
Lucia Rotiroti ◽  
Luca De Stefano
Keyword(s):  
Porous Silicon ◽  
Conformational Changes ◽  
Protein Conformational Changes ◽  
Spectroscopic Reflectometry

Nitrogenase iron-molybdenum cofactor binding site: Protein conformational changes associated with cofactor binding

Tetrahedron ◽  
1997 ◽  
Vol 53 (35) ◽  
pp. 11971-11984 ◽  
Author(s):  
Jon K. Magnuson ◽  
Timothy D. Paustian ◽  
Vinod K. Shah ◽  
Dennis R. Dean ◽  
Gary P. Roberts ◽  
...  
Keyword(s):  
Binding Site ◽  
Conformational Changes ◽  
Molybdenum Cofactor ◽  
Cofactor Binding ◽  
Protein Conformational Changes ◽  
Iron Molybdenum Cofactor
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