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  1. 1
    Insights into the local residual entropy of proteins provided by NMR relaxation

    Insights into the local residual entropy of proteins provided by NMR relaxation mā Zhigang Li, Soumya Raychaudhuri, A. Joshua Wand

    I whakaputaina 1996
    Whiwhi kuputuhi katoa
    Artigo
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  2. 2
    Temperature dependence of the hydrophobic interaction in protein folding.

    Temperature dependence of the hydrophobic interaction in protein folding. mā Robert L. Baldwin

    I whakaputaina 1986
    Whiwhi kuputuhi katoa
    Artigo
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  3. 3
    Large Scale Affinity Calculations of Cyclodextrin Host–Guest Complexes: Understanding the Role of Reorganization in the Molecular Recognition Process

    Large Scale Affinity Calculations of Cyclodextrin Host–Guest Complexes: Understanding the Role of Reorganization in the Molecular Recognition Process mā Lauren Wickstrom, Peng He, Emilio Gallicchio, Ronald M. Levy

    I whakaputaina 2013
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    Artigo
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  4. 4
    Extraction of configurational entropy from molecular simulations via an expansion approximation

    Extraction of configurational entropy from molecular simulations via an expansion approximation mā Benjamin J. Killian, Joslyn Yundenfreund Kravitz, Michael K. Gilson

    I whakaputaina 2007
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    Artigo
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  5. 5
    Estimating Absolute Configurational Entropies of Macromolecules: The Minimally Coupled Subspace Approach

    Estimating Absolute Configurational Entropies of Macromolecules: The Minimally Coupled Subspace Approach mā Ulf Hensen, Oliver F. Lange, Helmut Grubmüller

    I whakaputaina 2010
    Whiwhi kuputuhi katoa Whiwhi kuputuhi katoa
    Artigo
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  6. 6
    Configurational entropy of native proteins

    Configurational entropy of native proteins mā Martin Karplus, Toshiko Ichiye, B. Montgomery Pettitt

    I whakaputaina 1987
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  7. 7
    Entropy calculations on a reversibly folding peptide: Changes in solute free energy cannot explain folding behavior

    Entropy calculations on a reversibly folding peptide: Changes in solute free energy cannot explain folding behavior mā H. -J. Sch�fer, Xavier Daura, Alan E. Mark, Wilfred F. van Gunsteren

    I whakaputaina 2001
    Whiwhi kuputuhi katoa Whiwhi kuputuhi katoa
    Artigo
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  8. 8
    Side-chain entropy opposes alpha-helix formation but rationalizes experimentally determined helix-forming propensities.

    Side-chain entropy opposes alpha-helix formation but rationalizes experimentally determined helix-forming propensities. mā Trevor P. Creamer, George D. Rose

    I whakaputaina 1992
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    Artigo
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  9. 9
    Molecular dynamics simulations with replica-averaged structural restraints generate structural ensembles according to the maximum entropy principle

    Molecular dynamics simulations with replica-averaged structural restraints generate structural ensembles according to the maximum entropy principle mā Andrea Cavalli, Carlo Camilloni, Michele Vendruscolo

    I whakaputaina 2013
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    Artigo
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  10. 10
    Microscopic Insights into the NMR Relaxation-Based Protein Conformational Entropy Meter

    Microscopic Insights into the NMR Relaxation-Based Protein Conformational Entropy Meter mā Vignesh Kasinath, Kim A. Sharp, A. Joshua Wand

    I whakaputaina 2013
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    Artigo
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  11. 11
    Configurational entropy elucidates the role of salt‐bridge networks in protein thermostability

    Configurational entropy elucidates the role of salt‐bridge networks in protein thermostability mā J. Missimer, Michel O. Steinmetz, Riccardo Baron, Fritz K. Winkler, Richard A. Kammerer, Xavier Daura, Wilfred F. van Gunsteren

    I whakaputaina 2007
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    Artigo
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  12. 12
    Side‐chain conformational entropy in protein folding

    Side‐chain conformational entropy in protein folding mā Andrew J. Doig, Michael J.E. Sternberg

    I whakaputaina 1995
    Whiwhi kuputuhi katoa
    Revisão
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  13. 13
    Calculation of Cyclodextrin Binding Affinities: Energy, Entropy, and Implications for Drug Design

    Calculation of Cyclodextrin Binding Affinities: Energy, Entropy, and Implications for Drug Design mā Wei Chen, Chia‐en A. Chang, Michael K. Gilson

    I whakaputaina 2004
    Whiwhi kuputuhi katoa Whiwhi kuputuhi katoa
    Artigo
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  14. 14
    On the relationship between NMR-derived amide order parameters and protein backbone entropy changes

    On the relationship between NMR-derived amide order parameters and protein backbone entropy changes mā Kim A. Sharp, Evan S. O’Brien, Vignesh Kasinath, A. Joshua Wand

    I whakaputaina 2015
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    Artigo
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  15. 15
    Computational Methods for Configurational Entropy Using Internal and Cartesian Coordinates

    Computational Methods for Configurational Entropy Using Internal and Cartesian Coordinates mā Simon Hikiri, Takashi Yoshidome, Mitsunori Ikeguchi

    I whakaputaina 2016
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    Artigo
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  16. 16
    Entropy in molecular recognition by proteins

    Entropy in molecular recognition by proteins mā A. José, Kyle W. Harpole, Vignesh Kasinath, Jackwee Lim, Jeffrey M. Granja, Kathleen G. Valentine, Kim A. Sharp, A. Joshua Wand

    I whakaputaina 2017
    Whiwhi kuputuhi katoa Whiwhi kuputuhi katoa
    Artigo
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  17. 17
    Configurational Entropy in Protein–Peptide Binding:

    Configurational Entropy in Protein–Peptide Binding: mā Benjamin J. Killian, Joslyn Yudenfreund Kravitz, Sandeep Somani, Paramita Dasgupta, Yuan‐Ping Pang, Michael K. Gilson

    I whakaputaina 2009
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    Artigo
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  18. 18
    Measuring Entropy in Molecular Recognition by Proteins

    Measuring Entropy in Molecular Recognition by Proteins mā A. Joshua Wand, Kim A. Sharp

    I whakaputaina 2018
    Whiwhi kuputuhi katoa Whiwhi kuputuhi katoa
    Revisão
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  19. 19
    Interplay between Conformational Entropy and Solvation Entropy in Protein–Ligand Binding

    Interplay between Conformational Entropy and Solvation Entropy in Protein–Ligand Binding mā Maria Luisa Verteramo, Olof Stenström, Majda Misini Ignjatović, Octav Caldararu, Martin Olsson, Francesco Manzoni, Hakon Leffler, Esko Oksanen, Derek T. Logan, Ulf J. Nilsson, Ulf Ryde, Mikael Akke

    I whakaputaina 2019
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    Artigo
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  20. 20
    Entropy–Entropy Compensation between the Protein, Ligand, and Solvent Degrees of Freedom Fine-Tunes Affinity in Ligand Binding to Galectin-3C

    Entropy–Entropy Compensation between the Protein, Ligand, and Solvent Degrees of Freedom Fine-Tunes Affinity in Ligand Binding to Galectin-3C mā Johan Wallerstein, Vilhelm Ekberg, Majda Misini Ignjatović, Rohit Kumar, Octav Caldararu, Kristoffer Peterson, Sven Wernersson, Ulrika Brath, Hakon Leffler, Esko Oksanen, Derek T. Logan, Ulf J. Nilsson, Ulf Ryde, Mikael Akke

    I whakaputaina 2021
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    Artigo
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