Chemistry Reference
In-Depth Information
133. S. J. Hagen and W. A. Eaton, J. Mol. Biol. , 297 , 781 (2000). Two-State Expansion and
Collapse of a Polypeptide.
134. S. Akiyama, S. Takahashi, T. Kimura, K. Ishimori, I. Morishima, Y. Nishikawa, and
T. Fujisawa, Proc.Natl.Acad.Sci.U.S.A. , 99 , 1329 (2002). Conformational Land-
scape of Cytochrome c Folding Studied by Microsecond-Resolved Small-Angle X-Ray
Scattering.
135. J. G. Lyubovitsky, H. B. Gray, and J. R. Winkler, J. Am. Chem. Soc. , 124 , 14840 (2002).
Structural Features of the Cytochrome c Molten Globule Revealed by Fluorescence Energy
Transfer Kinetics.
136. J. S. Valentine and P. J. Hart, Proc. Natl. Acad. Sci. U.S.A. , 100 , 3617 (2003). Misfolded
Cuznsod and Amyotrophic Lateral Sclerosis.
137. R. W. Strange, S. V. Antonyuk, M. A. Hough, P. A. Doucette, J. S. Valentine, and S. S.
Hasnain, J. Mol. Biol. , 356 , 1152 (2006). Variable Metallation of Human Superoxide
Dismutase: Atomic Resolution Crystal Structures of Cu-Zn, Zn-Zn and as-Isolated Wild-
Type Enzymes.
138. R. W. Strange, S. Antonyuk, M. A. Hough, P. A. Doucette, J. A. Rodriguez, P. J. Hart, L. J.
Hayward, J. S. Valentine, and S. S. Hasnain, J. Mol. Biol. , 328 , 877 (2003). The Structure of
Holo and Metal-Deficient Wild-Type Human Cu, Zn Superoxide Dismutase and Its
Relevance to Familial Amyotrophic Lateral Sclerosis.
139. A. K. Faradjian and R. Elber, J. Chem. Phys. , 120 , 10880 (2004). Computing Time Scales from
Reaction Coordinates by Milestoning.
140. R. Elber, Biophys. J. , 92 , L85 (2007). A Milestoning Study of the Kinetics of an Allosteric
Transition: Atomically Detailed Simulations of Deoxy Scapharca Hemoglobin.
141. A. M. A. West, R. Elber, and D. Shalloway, J. Chem. Phys. , 126 , 145104 (2007). Extending
Molecular Dynamics Timescales with Milestoning: Example of Complex Kinetics in a
Solvated Peptide.
142. D. Moroni, P. G. Bolhuis, and T. S. van Erp, J. Chem. Phys. , 120 , 4055 (2004). Rate Constants
for Diffusive Processes by Partial Path Sampling.
Search WWH ::




Custom Search