| Year |
Citation |
Score |
| 2019 |
Fuglestad B, Gupta K, Wand AJ, Sharp KA. Water loading driven size, shape, and composition of cetyltrimethylammonium/hexanol/pentane reverse micelles. Journal of Colloid and Interface Science. 540: 207-217. PMID 30640068 DOI: 10.1016/J.Jcis.2019.01.016 |
0.309 |
|
| 2019 |
Sharp KA. Companion Simulations and Modeling to NMR-Based Dynamical Studies of Proteins. Methods in Enzymology. 615: 1-41. PMID 30638527 DOI: 10.1016/Bs.Mie.2018.08.038 |
0.32 |
|
| 2018 |
Wand AJ, Sharp KA. Measuring Entropy in Molecular Recognition by Proteins. Annual Review of Biophysics. PMID 29345988 DOI: 10.1146/Annurev-Biophys-060414-034042 |
0.397 |
|
| 2017 |
Caro JA, Harpole KW, Kasinath V, Lim J, Granja J, Valentine KG, Sharp KA, Wand AJ. Entropy in molecular recognition by proteins. Proceedings of the National Academy of Sciences of the United States of America. PMID 28584100 DOI: 10.1073/Pnas.1621154114 |
0.417 |
|
| 2016 |
O'Brien ES, Wand AJ, Sharp KA. On the ability of molecular dynamics force fields to recapitulate NMR derived protein side chain NMR order parameters. Protein Science : a Publication of the Protein Society. PMID 26990788 DOI: 10.1002/Pro.2922 |
0.332 |
|
| 2016 |
Sharp KA. Unpacking the origins of in-cell crowding. Proceedings of the National Academy of Sciences of the United States of America. 113: 1684-5. PMID 26862174 DOI: 10.1073/Pnas.1600098113 |
0.324 |
|
| 2016 |
Fuglestad B, Gupta K, Wand AJ, Sharp KA. Characterization of Cetyl Trimethylammonium Bromide/Hexanol Reverse Micelles by Experimentally Benchmarked Molecular Dynamics Simulations. Langmuir : the Acs Journal of Surfaces and Colloids. PMID 26840651 DOI: 10.1021/Acs.Langmuir.5B03981 |
0.366 |
|
| 2015 |
Sharp KA. Analysis of the size dependence of macromolecular crowding shows that smaller is better. Proceedings of the National Academy of Sciences of the United States of America. 112: 7990-5. PMID 26080429 DOI: 10.1073/Pnas.1505396112 |
0.352 |
|
| 2015 |
Sharp KA, O'Brien E, Kasinath V, Wand AJ. On the relationship between NMR-derived amide order parameters and protein backbone entropy changes. Proteins. 83: 922-30. PMID 25739366 DOI: 10.1002/Prot.24789 |
0.345 |
|
| 2015 |
Kasinath V, Fu Y, Sharp KA, Wand AJ. A sharp thermal transition of fast aromatic-ring dynamics in ubiquitin. Angewandte Chemie (International Ed. in English). 54: 102-7. PMID 25476230 DOI: 10.1002/Anie.201408220 |
0.323 |
|
| 2015 |
Kasinath V, Harpole KW, Moorman VR, Valentine KG, Frederick KK, Sharp KA, Wand J. Motion and Conformational Entropy in Protein Function: Creation of an NMR-Based Entropy Meter Biophysical Journal. 108: 60a. DOI: 10.1016/J.Bpj.2014.11.362 |
0.363 |
|
| 2014 |
Sharp KA. The remarkable hydration of the antifreeze protein Maxi: a computational study. The Journal of Chemical Physics. 141: 22D510. PMID 25494781 DOI: 10.1063/1.4896693 |
0.397 |
|
| 2014 |
Sharp KA, Kasinath V, Wand AJ. Banding of NMR-derived methyl order parameters: implications for protein dynamics. Proteins. 82: 2106-17. PMID 24677353 DOI: 10.1002/Prot.24566 |
0.354 |
|
| 2014 |
Sharp KA. Biochemistry. Protein folding, interrupted. Science (New York, N.Y.). 343: 743-4. PMID 24531963 DOI: 10.1126/Science.1249405 |
0.366 |
|
| 2013 |
Kasinath V, Sharp KA, Wand AJ. Microscopic insights into the NMR relaxation-based protein conformational entropy meter. Journal of the American Chemical Society. 135: 15092-100. PMID 24007504 DOI: 10.1021/Ja405200U |
0.359 |
|
| 2013 |
Sharp K. Calculation of molecular entropies using temperature integration Journal of Chemical Theory and Computation. 9: 1164-1172. DOI: 10.1021/Ct300901X |
0.311 |
|
| 2013 |
Kasinath V, Sharp KA, Wand JA. Molecular Dynamics Simulations Support the use of Methyl Generalized Order Parameters in the “Entropy Meter” Biophysical Journal. 104: 225a. DOI: 10.1016/J.Bpj.2012.11.1269 |
0.361 |
|
| 2012 |
Sharp KA. Chapter 22.4 Electrostatic interactions in proteins International Tables For Crystallography. DOI: 10.1107/97809553602060000888 |
0.412 |
|
| 2011 |
Harpole KW, Sharp KA. Calculation of configurational entropy with a Boltzmann-quasiharmonic model: the origin of high-affinity protein-ligand binding. The Journal of Physical Chemistry. B. 115: 9461-72. PMID 21678965 DOI: 10.1021/Jp111176X |
0.387 |
|
| 2011 |
Sharp KA. Allostery in the lac operon: population selection or induced dissociation? Biophysical Chemistry. 159: 66-72. PMID 21624765 DOI: 10.1016/J.Bpc.2011.05.007 |
0.359 |
|
| 2011 |
Sharp KA. A peek at ice binding by antifreeze proteins. Proceedings of the National Academy of Sciences of the United States of America. 108: 7281-2. PMID 21518869 DOI: 10.1073/Pnas.1104618108 |
0.358 |
|
| 2010 |
Zelent B, Sharp KA, Vanderkooi JM. Differential scanning calorimetry and fluorescence study of lactoperoxidase as a function of guanidinium-HCl, urea, and pH. Biochimica Et Biophysica Acta. 1804: 1508-15. PMID 20298816 DOI: 10.1016/J.Bbapap.2010.03.003 |
0.305 |
|
| 2010 |
Coleman RG, Sharp KA. Protein pockets: inventory, shape, and comparison. Journal of Chemical Information and Modeling. 50: 589-603. PMID 20205445 DOI: 10.1021/Ci900397T |
0.637 |
|
| 2010 |
Sharp KA, Vanderkooi JM. Water in the half shell: structure of water, focusing on angular structure and solvation. Accounts of Chemical Research. 43: 231-9. PMID 19845327 DOI: 10.1021/Ar900154J |
0.388 |
|
| 2010 |
Coleman RG, Sharp KA. Shape and evolution of thermostable protein structure. Proteins. 78: 420-33. PMID 19731381 DOI: 10.1002/Prot.22558 |
0.641 |
|
| 2009 |
Daber R, Sharp K, Lewis M. One is not enough. Journal of Molecular Biology. 392: 1133-44. PMID 19631220 DOI: 10.1016/J.Jmb.2009.07.050 |
0.301 |
|
| 2009 |
Zelent B, Bryan MA, Sharp KA, Vanderkooi JM. Influence of surface groups of proteins on water studied by freezing/thawing hysteresis and infrared spectroscopy. Biophysical Chemistry. 141: 222-30. PMID 19251353 DOI: 10.1016/J.Bpc.2009.02.002 |
0.385 |
|
| 2009 |
Coleman RG, Sharp KA. Finding and characterizing tunnels in macromolecules with application to ion channels and pores. Biophysical Journal. 96: 632-45. PMID 18849407 DOI: 10.1529/Biophysj.108.135970 |
0.589 |
|
| 2009 |
Yang Q, Sharp KA. Building alternate protein structures using the elastic network model. Proteins. 74: 682-700. PMID 18704927 DOI: 10.1002/Prot.22184 |
0.358 |
|
| 2009 |
Coleman RG, Sharp KA. Thermophilic protein structure adaptation examined with Burial Depth and Travel Depth Biophysical Journal. 96: 584a. DOI: 10.1016/J.Bpj.2008.12.3055 |
0.625 |
|
| 2008 |
Frederick KK, Sharp KA, Warischalk N, Wand AJ. Re-evaluation of the model-free analysis of fast internal motion in proteins using NMR relaxation. The Journal of Physical Chemistry. B. 112: 12095-103. PMID 18759409 DOI: 10.1021/Jp8038576 |
0.339 |
|
| 2008 |
Prabhu NV, Panda M, Yang Q, Sharp KA. Explicit ion, implicit water solvation for molecular dynamics of nucleic acids and highly charged molecules. Journal of Computational Chemistry. 29: 1113-30. PMID 18074338 DOI: 10.1002/Jcc.20874 |
0.339 |
|
| 2007 |
Song XJ, Flynn PF, Sharp KA, Wand AJ. Temperature dependence of fast dynamics in proteins. Biophysical Journal. 92: L43-5. PMID 17218465 DOI: 10.1529/Biophysj.106.102160 |
0.319 |
|
| 2006 |
Yang Q, Sharp KA. Atomic Charge Parameters for the Finite Difference Poisson-Boltzmann Method Using Electronegativity Neutralization. Journal of Chemical Theory and Computation. 2: 1152-67. PMID 26633072 DOI: 10.1021/Ct060009C |
0.357 |
|
| 2006 |
Coleman RG, Sharp KA. Travel depth, a new shape descriptor for macromolecules: application to ligand binding. Journal of Molecular Biology. 362: 441-58. PMID 16934837 DOI: 10.1016/J.Jmb.2006.07.022 |
0.631 |
|
| 2006 |
Sharp K, Skinner JJ. Pump-probe molecular dynamics as a tool for studying protein motion and long range coupling Proteins: Structure, Function and Genetics. 65: 347-361. PMID 16933296 DOI: 10.1002/Prot.21146 |
0.358 |
|
| 2006 |
Dashnau JL, Nucci NV, Sharp KA, Vanderkooi JM. Hydrogen bonding and the cryoprotective properties of glycerol/water mixtures. The Journal of Physical Chemistry. B. 110: 13670-7. PMID 16821896 DOI: 10.1021/Jp0618680 |
0.325 |
|
| 2006 |
Prabhu N, Sharp K. Protein-solvent interactions Chemical Reviews. 106: 1616-1623. PMID 16683747 DOI: 10.1021/Cr040437F |
0.416 |
|
| 2006 |
Sharp KA. Electrostatic interactions in proteins International Tables For Crystallography. DOI: 10.1107/97809553602060000712 |
0.403 |
|
| 2005 |
Dashnau JL, Sharp KA, Vanderkooi JM. Carbohydrate intramolecular hydrogen bonding cooperativity and its effect on water structure. The Journal of Physical Chemistry. B. 109: 24152-9. PMID 16375407 DOI: 10.1021/Jp0543072 |
0.35 |
|
| 2005 |
Prabhu NV, Sharp KA. Heat capacity in proteins. Annual Review of Physical Chemistry. 56: 521-48. PMID 15796710 DOI: 10.1146/Annurev.Physchem.56.092503.141202 |
0.383 |
|
| 2005 |
Yang C, Sharp KA. Hydrophobic tendency of polar group hydration as a major force in type I antifreeze protein recognition. Proteins. 59: 266-74. PMID 15726609 DOI: 10.1002/Prot.20429 |
0.391 |
|
| 2004 |
Prabhu NV, Zhu P, Sharp KA. Implementation and testing of stable, fast implicit solvation in molecular dynamics using the smooth-permittivity finite difference Poisson-Boltzmann method. Journal of Computational Chemistry. 25: 2049-64. PMID 15481091 DOI: 10.1002/Jcc.20138 |
0.386 |
|
| 2004 |
Yang C, Sharp KA. The mechanism of the type III antifreeze protein action: a computational study. Biophysical Chemistry. 109: 137-48. PMID 15059666 DOI: 10.1016/J.Bpc.2003.10.024 |
0.413 |
|
| 2004 |
Zelent B, Kaposi AD, Nucci NV, Sharp KA, Dalosto SD, Wright WW, Vanderkooi JM. Water channel of horseradish peroxidase studied by the charge-transfer absorption band of ferric heme Journal of Physical Chemistry B. 108: 10317-10324. DOI: 10.1021/Jp037664Q |
0.35 |
|
| 2003 |
Khajehpour M, Rietveld I, Vinogradov S, Prabhu NV, Sharp KA, Vanderkooi JM. Accessibility of oxygen with respect to the heme pocket in horseradish peroxidase. Proteins. 53: 656-66. PMID 14579357 DOI: 10.1002/Prot.10475 |
0.347 |
|
| 2003 |
Kaposi AD, Prabhu NV, Dalosto SD, Sharp KA, Wright WW, Stavrov SS, Vanderkooi JM. Solvent dependent and independent motions of CO-horseradish peroxidase examined by infrared spectroscopy and molecular dynamics calculations. Biophysical Chemistry. 106: 1-14. PMID 14516907 DOI: 10.1016/S0301-4622(03)00122-4 |
0.359 |
|
| 2003 |
Gallagher KR, Sharp KA. Analysis of thermal hysteresis protein hydration using the random network model. Biophysical Chemistry. 105: 195-209. PMID 14499892 DOI: 10.1016/S0301-4622(03)00087-5 |
0.741 |
|
| 2003 |
Gallagher KR, Sharp KA. A new angle on heat capacity changes in hydrophobic solvation. Journal of the American Chemical Society. 125: 9853-60. PMID 12904053 DOI: 10.1021/Ja029796N |
0.73 |
|
| 2003 |
Prabhu NV, Lee AL, Wand AJ, Sharp KA. Dynamics and entropy of a calmodulin-peptide complex studied by NMR and molecular dynamics. Biochemistry. 42: 562-70. PMID 12525185 DOI: 10.1021/Bi026544Q |
0.335 |
|
| 2003 |
Dalosto SD, Prabhu NV, Vanderkooi JM, Sharp KA. A density functional theory study of conformers in the ferrous CO complex of horseradish peroxidase with distinct Fe-C-O configurations Journal of Physical Chemistry B. 107: 1884-1892. DOI: 10.1021/Jp022018X |
0.35 |
|
| 2002 |
Lee AL, Sharp KA, Kranz JK, Song XJ, Wand AJ. Temperature dependence of the internal dynamics of a calmodulin-peptide complex. Biochemistry. 41: 13814-25. PMID 12427045 DOI: 10.1021/Bi026380D |
0.332 |
|
| 2002 |
Brooijmans N, Sharp KA, Kuntz ID. Stability of macromolecular complexes. Proteins. 48: 645-53. PMID 12211032 DOI: 10.1002/Prot.10139 |
0.402 |
|
| 2002 |
Luo H, Sharp K. On the calculation of absolute macromolecular binding free energies Proceedings of the National Academy of Sciences of the United States of America. 99: 10399-10404. PMID 12149474 DOI: 10.1073/Pnas.162365999 |
0.342 |
|
| 2002 |
Sale K, Sár C, Sharp KA, Hideg K, Fajer PG. Structural determination of spin label immobilization and orientation: a Monte Carlo minimization approach. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 156: 104-12. PMID 12081447 DOI: 10.1006/Jmre.2002.2529 |
0.348 |
|
| 2002 |
Prabhu NV, Dalosto SD, Sharp KA, Wright WW, Vanderkooi JM. Optical spectra of Fe(II) cytochrome c interpreted using molecular dynamics simulations and quantum mechanical calculations Journal of Physical Chemistry B. 106: 5561-5571. DOI: 10.1021/Jp014208Y |
0.38 |
|
| 2002 |
Sharp KA. Electrostatic interactions in proteins. Progress in Clinical and Biological Research. 289: 199-235. DOI: 10.1007/0-306-46934-0_5 |
0.332 |
|
| 2001 |
Madan B, Sharp KA. Hydration heat capacity of nucleic acid constituents determined from the random network model Biophysical Journal. 81: 1881-1887. PMID 11566762 DOI: 10.1016/S0006-3495(01)75839-0 |
0.398 |
|
| 2001 |
Sharp K. Entropy-enthalpy compensation: Fact or artifact? Protein Science. 10: 661-667. PMID 11344335 DOI: 10.1110/Ps.37801 |
0.34 |
|
| 2001 |
Sharp KA, Madan B, Manas E, Vanderkooi JM. Water structure changes induced by hydrophobic and polar solutes revealed by simulations and infrared spectroscopy Journal of Chemical Physics. 114: 1791-1796. DOI: 10.1063/1.1334678 |
0.373 |
|
| 2001 |
Madan B, Sharp K. Heat Capacity Changes Accompanying Hydrophobic and Ionic Solvation: A Monte-Carlo and Random Network Model Study The Journal of Physical Chemistry B. 105: 2256-2256. DOI: 10.1021/Jp003954K |
0.35 |
|
| 2001 |
Rasnik I, Sharp KA, Fee JA, Vanderkooi JM. Spectral analysis of cytochrome c: Effect of heme conformation, axial ligand, peripheral substituents, and local electric fields Journal of Physical Chemistry B. 105: 282-286. DOI: 10.1021/Jp002656K |
0.317 |
|
| 2000 |
Manas ES, Wright WW, Sharp KA, Friedrich J, Vanderkooi JM. The influence of protein environment on the low temperature electronic spectroscopy of Zn-substituted cytochrome Journal of Physical Chemistry B. 104: 6932-6941. DOI: 10.1021/Jp0005975 |
0.323 |
|
| 1999 |
Chin K, Sharp KA, Honig B, Pyle AM. Calculating the electrostatic properties of RNA provides new insights into molecular interactions and function. Nature Structural Biology. 6: 1055-61. PMID 10542099 DOI: 10.1038/14940 |
0.321 |
|
| 1999 |
Kuntz ID, Chen K, Sharp KA, Kollman PA. The maximal affinity of ligands. Proceedings of the National Academy of Sciences of the United States of America. 96: 9997-10002. PMID 10468550 DOI: 10.1073/Pnas.96.18.9997 |
0.339 |
|
| 1999 |
Madan B, Sharp K. Changes in water structure induced by a hydrophobic solute probed by simulation of the water hydrogen bond angle and radial distribution functions Biophysical Chemistry. 78: 33-41. PMID 10343383 DOI: 10.1016/S0301-4622(98)00227-0 |
0.323 |
|
| 1999 |
Dieckmann GR, Lear JD, Zhong Q, Klein ML, DeGrado WF, Sharp KA. Exploration of the structural features defining the conduction properties of a synthetic ion channel Biophysical Journal. 76: 618-630. PMID 9929468 DOI: 10.1016/S0006-3495(99)77230-9 |
0.331 |
|
| 1999 |
Manas ES, Yanderkooi JM, Sharp KA. The effects of protein environment on the low temperature electronic spectroscopy of cytochrome c and microperoxidase-11 Journal of Physical Chemistry B. 103: 6334-6348. DOI: 10.1021/Jp9908552 |
0.317 |
|
| 1998 |
Sharp KA. Calculation of HyHel10-lysozyme binding free energy changes: Effect of ten point mutations Proteins: Structure, Function and Genetics. 33: 39-48. PMID 9741843 DOI: 10.1002/(Sici)1097-0134(19981001)33:1<39::Aid-Prot4>3.0.Co;2-G |
0.389 |
|
| 1998 |
Gallagher K, Sharp K. Electrostatic contributions to heat capacity changes of DNA-ligand binding Biophysical Journal. 75: 769-776. PMID 9675178 DOI: 10.1016/S0006-3495(98)77566-6 |
0.729 |
|
| 1998 |
Dieckmann GR, McRorie DK, Lear JD, Sharp KA, DeGrado WF, Pecoraro VL. The role of protonation and metal chelation preferences in defining the properties of mercury-binding coiled coils. Journal of Molecular Biology. 280: 897-912. PMID 9671558 DOI: 10.1006/Jmbi.1998.1891 |
0.317 |
|
| 1998 |
Laberge M, Sharp KA, Vanderkooi JM. Effect of charge interactions on the carboxylate vibrational stretching frequency in c-type cytochromes investigated by continuum electrostatic calculations and FTIR spectroscopy Biophysical Chemistry. 71: 9-20. PMID 9591357 DOI: 10.1016/S0301-4622(97)00127-0 |
0.328 |
|
| 1998 |
Sharp KA. Calculation of electron transfer reorganization energies using the finite difference Poisson-Boltzmann model Biophysical Journal. 74: 1241-1250. PMID 9512022 DOI: 10.1016/S0006-3495(98)77838-5 |
0.355 |
|
| 1998 |
Vanzi F, Madan B, Sharp K. Effect of the protein denaturants urea and guanidinium on water structure: A structural and thermodynamic study Journal of the American Chemical Society. 120: 10748-10753. DOI: 10.1021/Ja981529N |
0.37 |
|
| 1997 |
Novotny J, Bruccoleri RE, Davis M, Sharp KA. Empirical free energy calculations: A blind test and further improvements to the method Journal of Molecular Biology. 268: 401-411. PMID 9159479 DOI: 10.1006/Jmbi.1997.0961 |
0.357 |
|
| 1997 |
Brady GP, Sharp KA. Entropy in protein folding and in protein-protein interactions Current Opinion in Structural Biology. 7: 215-221. PMID 9094326 DOI: 10.1016/S0959-440X(97)80028-0 |
0.406 |
|
| 1997 |
Brady GP, Sharp KA. Energetics of cyclic dipeptide crystal packing and solvation Biophysical Journal. 72: 913-927. PMID 9017216 DOI: 10.1016/S0006-3495(97)78725-3 |
0.337 |
|
| 1997 |
Madan B, Sharp K. Molecular Origin of Hydration Heat Capacity Changes of Hydrophobic Solutes: Perturbation of Water Structure around Alkanes The Journal of Physical Chemistry B. 101: 11237-11242. DOI: 10.1021/Jp972456H |
0.374 |
|
| 1997 |
Laberge M, Sharp KA, Vanderkooi JM. Protein electric field effects on the CO stretch frequency of carbonmonoxycytochromes c as a function of carbonyl tilting and bending investigated with a continuum electrostatic approach Journal of Physical Chemistry B. 101: 7364-7367. DOI: 10.1021/Jp9706846 |
0.333 |
|
| 1997 |
Sharp KA, Madan B. Hydrophobic effect, water structure, and heat capacity changes Journal of Physical Chemistry B. 101: 4343-4348. DOI: 10.1021/Jp9702457 |
0.386 |
|
| 1997 |
Bruccoleri RE, Novotny J, Davis ME, Sharp KA. Finite difference Poisson-Boltzmann electrostatic calculations: Increased accuracy achieved by harmonic dielectric smoothing and charge antialiasing Journal of Computational Chemistry. 18: 268-276. DOI: 10.1002/(Sici)1096-987X(19970130)18:2<268::Aid-Jcc11>3.0.Co;2-E |
0.35 |
|
| 1996 |
Sharp KA. Electrostatic interactions in hirudin-thrombin binding Biophysical Chemistry. 61: 37-49. PMID 8855358 DOI: 10.1016/0301-4622(96)00021-X |
0.34 |
|
| 1996 |
Sharp KA, Kumar S, Rossky PJ, Friedman RA, Honig B. Size dependence of transfer free energies. 2. Hard sphere models Journal of Physical Chemistry. 100: 14166-14177. DOI: 10.1021/Jp960668T |
0.329 |
|
| 1996 |
Laberge M, Vanderkooi JM, Sharp KA. Effect of a protein electric field on the CO stretch frequency. Finite difference Poisson-Boltzmann calculations on carbonmonoxycytochromes c Journal of Physical Chemistry. 100: 10793-10801. DOI: 10.1021/Jp960055G |
0.359 |
|
| 1995 |
Peitzsch RM, Eisenberg M, Sharp KA, McLaughlin S. Calculations of the electrostatic potential adjacent to model phospholipid bilayers Biophysical Journal. 68: 729-738. PMID 7756540 DOI: 10.1016/S0006-3495(95)80253-5 |
0.318 |
|
| 1995 |
Sharp KA, Honig B. Salt effects on nucleic acids Current Opinion in Structural Biology. 5: 323-328. PMID 7583630 DOI: 10.1016/0959-440X(95)80093-X |
0.359 |
|
| 1995 |
Sharp KA, Friedman RA, Misra V, Hecht J, Honig B. Salt effects on polyelectrolyte–ligand binding: Comparison of Poisson–Boltzmann, and limiting law/counterion binding models Biopolymers. 36: 245-262. PMID 7492748 DOI: 10.1002/Bip.360360211 |
0.384 |
|
| 1995 |
Brady GP, Sharp KA. Decomposition of interaction free energies in proteins and other complex systems Journal of Molecular Biology. 254: 77-85. PMID 7473761 DOI: 10.1006/Jmbi.1995.0600 |
0.302 |
|
| 1995 |
Sridharan S, Nicholls A, Sharp KA. A rapid method for calculating derivatives of solvent accessible surface areas of molecules Journal of Computational Chemistry. 16: 1038-1044. DOI: 10.1002/Jcc.540160810 |
0.327 |
|
| 1995 |
Sharp KA. Polyelectrolyte electrostatics: Salt dependence, entropic, and enthalpic contributions to free energy in the nonlinear Poisson-Boltzmann model Biopolymers. 36: 227-243. DOI: 10.1002/Bip.360360210 |
0.375 |
|
| 1994 |
Misra VK, Hecht JL, Sharp KA, Friedman RA, Honig B. Salt effects on protein-DNA interactions: The λcI repressor and EcoRI endonuclease Journal of Molecular Biology. 238: 264-280. PMID 8158653 DOI: 10.1006/Jmbi.1994.1286 |
0.39 |
|
| 1994 |
Sitkoff D, Sharp KA, Honig B. Correlating solvation free energies and surface tensions of hydrocarbon solutes Biophysical Chemistry. 51: 397-409. PMID 7919044 DOI: 10.1016/0301-4622(94)00062-X |
0.356 |
|
| 1994 |
Sharp KA, Englander SW. How much is a stabilizing bond worth? Trends in Biochemical Sciences. 19: 526-9. PMID 7846760 DOI: 10.1016/0968-0004(94)90051-5 |
0.329 |
|
| 1994 |
Sitkoff D, Lockhart DJ, Sharp KA, Honig B. Calculation of electrostatic effects at the amino terminus of an α helix Biophysical Journal. 67: 2251-2260. PMID 7696466 DOI: 10.1016/S0006-3495(94)80709-X |
0.372 |
|
| 1994 |
Misra VK, Sharp KA, Friedman RA, Honig B. Salt effects on ligand-DNA binding: Minor groove binding antibiotics Journal of Molecular Biology. 238: 245-263. PMID 7512653 DOI: 10.1006/Jmbi.1994.1285 |
0.352 |
|
| 1994 |
Sitkoff D, Sharp KA, Honig B. Accurate Calculation of Hydration Free Energies Using Macroscopic Solvent Models The Journal of Physical Chemistry. 98: 1978-1988. DOI: 10.1021/J100058A043 |
0.381 |
|
| 1994 |
Sharp KA. Electrostatic interactions in macromolecules Current Opinion in Structural Biology. 4: 234-239. DOI: 10.1016/S0959-440X(94)90314-X |
0.333 |
|
| 1993 |
Yang AS, Gunner MR, Sampogna R, Sharp K, Honig B. On the calculation of pK(a)s in proteins Proteins: Structure, Function and Genetics. 15: 252-265. PMID 7681210 DOI: 10.1002/Prot.340150304 |
0.366 |
|
| 1993 |
Honig B, Sharp K, Yang AS. Macroscopic Models of Aqueous Solutions: Biological and Chemical Applications The Journal of Physical Chemistry. 97: 1101-1109. DOI: 10.1021/J100108A002 |
0.32 |
|
| 1992 |
Yang AS, Sharp KA, Honig B. Analysis of the heat capacity dependence of protein folding Journal of Molecular Biology. 227: 889-900. PMID 1404393 DOI: 10.1016/0022-2836(92)90229-D |
0.416 |
|
| 1991 |
Sharp KA, Nicholls A, Fine RF, Honig B. Reconciling the magnitude of the microscopic and macroscopic hydrophobic effects Science. 252: 106-109. PMID 2011744 DOI: 10.1126/Science.2011744 |
0.383 |
|
| 1991 |
Sharp KA, Nicholls A, Friedman R, Honig B. Extracting hydrophobic free energies from experimental data: relationship to protein folding and theoretical models. Biochemistry. 30: 9686-9697. PMID 1911756 DOI: 10.1021/Bi00104A017 |
0.422 |
|
| 1991 |
Sharp KA. Linkage of thioredoxin stability to titration of ionizable groups with perturbed pKa Biochemistry®. 30: 7609-7614. PMID 1906744 DOI: 10.1021/Bi00244A033 |
0.377 |
|
| 1991 |
Nicholls A, Sharp KA, Honig B. Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons Proteins: Structure, Function and Genetics. 11: 281-296. PMID 1758883 DOI: 10.1002/Prot.340110407 |
0.44 |
|
| 1991 |
Sharp KA. The hydrophobic effect Current Opinion in Structural Biology. 1: 171-174. DOI: 10.1016/0959-440X(91)90057-Z |
0.375 |
|
| 1991 |
Sharp K. Incorporating solvent and ion screening into molecular dynamics using the finite-difference Poisson-Boltzmann method Journal of Computational Chemistry. 12: 454-468. DOI: 10.1002/Jcc.540120407 |
0.372 |
|
| 1990 |
Sharp KA, Honig B, Harvey SC. Electrical potential of transfer RNAs: codon-anticodon recognition. Biochemistry. 29: 340-6. PMID 2405900 DOI: 10.1021/Bi00454A006 |
0.328 |
|
| 1990 |
Jayaram B, Swaminathan S, Beveridge DL, Sharp K, Honig B. Monte Carlo simulation studies on the structure of the counterion atmosphere of B-DNA. Variations on the primitive dielectric model Macromolecules. 23: 3156-3165. DOI: 10.1021/Ma00214A021 |
0.35 |
|
| 1989 |
Jayaram B, Sharp KA, Honig B. The electrostatic potential of B-DNA Biopolymers. 28: 975-993. PMID 2742988 DOI: 10.1002/Bip.360280506 |
0.357 |
|
| 1988 |
Gilson MK, Sharp KA, Honig BH. Calculating the electrostatic potential of molecules in solution: Method and error assessment Journal of Computational Chemistry. 9: 327-335. DOI: 10.1002/Jcc.540090407 |
0.329 |
|
| 1986 |
McDaniel RV, Sharp K, Brooks D, McLaughlin AC, Winiski AP, Cafiso D, McLaughlin S. Electrokinetic and electrostatic properties of bilayers containing gangliosides GM1, GD1a, or GT1. Comparison with a nonlinear theory. Biophysical Journal. 49: 741-52. PMID 3697476 DOI: 10.1016/S0006-3495(86)83700-6 |
0.331 |
|
| 1986 |
Klapper I, Hagstrom R, Fine R, Sharp K, Honig B. Focusing of electric fields in the active site of Cu‐Zn superoxide dismutase: Effects of ionic strength and amino‐acid modification Proteins. 1: 47-59. PMID 3449851 DOI: 10.1002/Prot.340010109 |
0.363 |
|
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