Hydrophobic moment of multi-domain proteins

Data processing: structural design – modeling – simulation – and em – Simulating nonelectrical device or system – Biological or biochemical

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C702S019000

Reexamination Certificate

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08010332

ABSTRACT:
Techniques for protein structure analysis are provided. In one aspect, an apparatus for characterizing a multi-domain protein structure comprises the following steps. For at least one domain, a hydrophobic dipole, e.g., defined as a first-order hydrophobic moment of the domain, is calculated. A score representing the orientation of the hydrophobic dipole of the at least one domain relative to a hydrophobic dipole of one or more other domains of the multi-domain protein structure is then calculated.

REFERENCES:
Eisenberg et al. “Hydrophobic moments and protein structure” Faraday Symp. Chem. Soc., (1982) vol. 17, pp. 107-120.
Karplus “Hydrophobicity Regained” Protein Science (1997) vol. 6, pp. 1302-1307.
R. Jaenicke, Stability and Folding of Domain Proteins, 71 Prog. Biophys. & Mol. Biol. 155-241 (1999).
C. Anselmi, et al., Identification of Protein Domains on Topological Basis, 58 Biopolymers 218-229 (2001).
S.J. Wheelan et al., Domain Size Distributions Can Predict Domain Boundaries, 16 Bioinformatics 613-618 (2000).
A.G. Murzin et al., SCOP: A Structural Classification of Protein Database for the Investigation of Sequences and Structures, 247 J. Mol. Biol. 536-540 (1995).
B.D. Silverman, Hydrophobic Moments of Protein Structures: Spatially Profiling the Distribution, 98 Proc. Natl. Acad. Sci. USA 4996-5001 (2001).
R. Zhou et al., Spatial Profiling of Protein Hydrophobicity: Native vs. Decoy Structures, 52 Proteins: Struc. Funct. & Genetics 561-572 (2003).
D. Eisenberg et al., The Helical Hydrophobic Moment: A Measure of the Amphiphilicity of a Helix, 299 Nature 371-374 (1982).
D. Eisenberg et al., Analysis of Membrane Protein Sequences with the Hydrophobic Moment Plot, 179 J. Mol. Biol. 125-142 (1984).
H.J. Pownall et al., Helical Amphipathic Moment: Application to Plasma Lipoproteins, 159 FEBS 17-23 (1983).
I. Tsigelny at al., Mechanism of Action of Chromogranin A On Catecholamine Release: Molecular Modeling of the Catestatin Region Reveals a -strand/loop/ -strand Structure Secured by Hydrophobic Interactions and Predictive of Activity, 77 Regulatory Peptides 43-53 (1998).
J.P. Pardo et al., An Alternative Model for the Transmembrane Segments of the Yeast H+-ATPase, 15 Yeast 1585-1593 (1999).
P.W. Mobley et al., Membrane Interactions of the Synthetic N-Terminal Peptide of HIV-1 gp41 and Its Structural Analogs, 1418 Biochimica et Biophysica Acta 1-18 (1999).
L. Thong et al., Flexible Programs for the Prediction of Average Amphiphilicity of Multiply Aligned Homologous Proteins: Application to Integral Membrane Transport Proteins, 16 Molecular Membrane Biology 173-179 (1999).
X. Gallet et al., A Fast Method to Predict Protein Interaction Sites from Sequences, 302 J. Mol. Biol. 917-926 (2000).
D.A. Phoenix et al., The Hydrophobic Moment and Its Use In The Classification of Amphiphilic Structures (Review), 19 Molecular Membrane Biology 1-10 (2002).
H. Zhou et al., The Stability Scale and Atomic Solvation Parameters Extracted From 1023 Mutation Experiments, 49 Proteins: Struc. Funct. & Genetics 483-492 (2002).

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