F11. General Links and References
- Page ID
- 4774
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\(\newcommand{\avec}{\mathbf a}\) \(\newcommand{\bvec}{\mathbf b}\) \(\newcommand{\cvec}{\mathbf c}\) \(\newcommand{\dvec}{\mathbf d}\) \(\newcommand{\dtil}{\widetilde{\mathbf d}}\) \(\newcommand{\evec}{\mathbf e}\) \(\newcommand{\fvec}{\mathbf f}\) \(\newcommand{\nvec}{\mathbf n}\) \(\newcommand{\pvec}{\mathbf p}\) \(\newcommand{\qvec}{\mathbf q}\) \(\newcommand{\svec}{\mathbf s}\) \(\newcommand{\tvec}{\mathbf t}\) \(\newcommand{\uvec}{\mathbf u}\) \(\newcommand{\vvec}{\mathbf v}\) \(\newcommand{\wvec}{\mathbf w}\) \(\newcommand{\xvec}{\mathbf x}\) \(\newcommand{\yvec}{\mathbf y}\) \(\newcommand{\zvec}{\mathbf z}\) \(\newcommand{\rvec}{\mathbf r}\) \(\newcommand{\mvec}{\mathbf m}\) \(\newcommand{\zerovec}{\mathbf 0}\) \(\newcommand{\onevec}{\mathbf 1}\) \(\newcommand{\real}{\mathbb R}\) \(\newcommand{\twovec}[2]{\left[\begin{array}{r}#1 \\ #2 \end{array}\right]}\) \(\newcommand{\ctwovec}[2]{\left[\begin{array}{c}#1 \\ #2 \end{array}\right]}\) \(\newcommand{\threevec}[3]{\left[\begin{array}{r}#1 \\ #2 \\ #3 \end{array}\right]}\) \(\newcommand{\cthreevec}[3]{\left[\begin{array}{c}#1 \\ #2 \\ #3 \end{array}\right]}\) \(\newcommand{\fourvec}[4]{\left[\begin{array}{r}#1 \\ #2 \\ #3 \\ #4 \end{array}\right]}\) \(\newcommand{\cfourvec}[4]{\left[\begin{array}{c}#1 \\ #2 \\ #3 \\ #4 \end{array}\right]}\) \(\newcommand{\fivevec}[5]{\left[\begin{array}{r}#1 \\ #2 \\ #3 \\ #4 \\ #5 \\ \end{array}\right]}\) \(\newcommand{\cfivevec}[5]{\left[\begin{array}{c}#1 \\ #2 \\ #3 \\ #4 \\ #5 \\ \end{array}\right]}\) \(\newcommand{\mattwo}[4]{\left[\begin{array}{rr}#1 \amp #2 \\ #3 \amp #4 \\ \end{array}\right]}\) \(\newcommand{\laspan}[1]{\text{Span}\{#1\}}\) \(\newcommand{\bcal}{\cal B}\) \(\newcommand{\ccal}{\cal C}\) \(\newcommand{\scal}{\cal S}\) \(\newcommand{\wcal}{\cal W}\) \(\newcommand{\ecal}{\cal E}\) \(\newcommand{\coords}[2]{\left\{#1\right\}_{#2}}\) \(\newcommand{\gray}[1]{\color{gray}{#1}}\) \(\newcommand{\lgray}[1]{\color{lightgray}{#1}}\) \(\newcommand{\rank}{\operatorname{rank}}\) \(\newcommand{\row}{\text{Row}}\) \(\newcommand{\col}{\text{Col}}\) \(\renewcommand{\row}{\text{Row}}\) \(\newcommand{\nul}{\text{Nul}}\) \(\newcommand{\var}{\text{Var}}\) \(\newcommand{\corr}{\text{corr}}\) \(\newcommand{\len}[1]{\left|#1\right|}\) \(\newcommand{\bbar}{\overline{\bvec}}\) \(\newcommand{\bhat}{\widehat{\bvec}}\) \(\newcommand{\bperp}{\bvec^\perp}\) \(\newcommand{\xhat}{\widehat{\xvec}}\) \(\newcommand{\vhat}{\widehat{\vvec}}\) \(\newcommand{\uhat}{\widehat{\uvec}}\) \(\newcommand{\what}{\widehat{\wvec}}\) \(\newcommand{\Sighat}{\widehat{\Sigma}}\) \(\newcommand{\lt}{<}\) \(\newcommand{\gt}{>}\) \(\newcommand{\amp}{&}\) \(\definecolor{fillinmathshade}{gray}{0.9}\)- Bartlett, G. et al. n to pi* interactions in protein. Nature Chemical Biology. 6, pg 615 (2010).
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- Silverstein, T. Hydrophobic Effect: J. Chem Ed. 85. 917-918 (2008)
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- Berezovsky, I & Shakhnovich, E. Physics and Evolution of Thermophilic Adaptation. PNAS 102, 12742 (2005)
- Beeby et al. The genomics of disulfide bonding and protein stabilization in themophiles. PLoS Biology. 3, 1549 (2005)
- Courtenay, E. et al. Thermodynamics of interactions of urea and guanidinium salts with protein surfaces: relationship between solute effects on protein processes and charges in water-accessible surface area. Protein Science. 10, 2485 (2001)
- Korkrgian, A. et al. Computational Thermostabilzation of an Enzyme. Science. 308, pg 857 (2005)
- Kashefi, K. and Lovley, D. Extending the Upper Temperature Limit for Life. Science. 301, pg 934 (2003).
- Omta et al. Negligible Effect of Ions on the Hydrogen-bond structure in liquid water. Science, g 347, 320 (2003)
- Dixit et al. Molecular degregation observed in a concentrated alcohol-water solution. Nature. 416, pg 829 (2002)
- Pace, C.N. Polar Group Burial Contributes More to Protein Stability than Nonpolar Group Burial. Biochemistry. 40, pg 310 (2001)
- Water at the Nanoscale (How water enters a hydrophobic nanotube - a molecular dynamics simulation) . Nature. 294414, pg 156, 188 (2001)
- Shortle & Ackerman. Persistence of Native-Like Topology in a Denatured Protein in 8 M Urea. Science. 293. pg 487 (2001)
- Brooks et al. Taking a Walk on a Landscape (about protein foldiing) Science, 293, pg 612 (2001)
- Chemistry Beyond the Molecule (supramolecular chemistry). Nature. 412, pg 397 (2001)
- Fernandez-Lopez et al. Rings of Destruction. (Cyclic peptides as drugs). Nature. 412 pg 392, 452 (2001)
- Scatena et al. Water at Hydrophobic Surfaces: Weak Hydrogren Bonding and Strong Orientation Effects. Science. 292. pg 908 (2001)
- Maritan et al. Best Packing in Proteins and DNA. Nature, 406, pg 251, 287 (2000)
- Oh et al. Folding-Driven synthesis of oligomers. Nature. 414, pg 889 (2001)
- Molecules at the Edge (solvent interactions at interfaces) Nature. 410, pg 645 (2001)
- Oesterhelt et al. Unraveling a membrane protein (denaturing a protein with atomic force microscopy). Science. 288, pg 63, 143 (2000)
- Sohl et al. Unfolded conformations of a-lytic protease are more stable that its native state. (has large kinetic barrier to unfolding). Nature. 395, pg 817 (1998)
- Pascher et al. Protein folding triggered by electron transfer. Science. 271, pg 1558 (1996)
- Koide et al. Design of a single-layer b-sheet without a hydrophobic core. Nature. 403, pg 456 (2000)
- Nelson et al. Solvophobically driven folding of nonbiological oligomers. Science. 277, pg 1793 (1997)
- Pace,C. N. et al. Forces contributing to the conformational stability of proteins. FASEB Jouranl. 10, 7583 (1996)


