Biblio

Found 20 results
Filters: Keyword is Thermodynamics  [Clear All Filters]
2022
Gisonno RA, Masson T, Ramella NA, Barrera EE, Romanowski V, M Tricerri A.  2022.  Evolutionary and structural constraints influencing apolipoprotein A-I amyloid behavior.. Proteins. 90(1):258-269.
Van Der Kant R, Louros N, Schymkowitz J, Rousseau F.  2022.  Thermodynamic analysis of amyloid fibril structures reveals a common framework for stability in amyloid polymorphs.. Structure. 30(8):1178-1189.e3.
2020
Yang J, Naik N, Patel JSuresh, Wylie CS, Gu W, Huang J, F Ytreberg M, Naik MT, Weinreich DM, Rubenstein BM.  2020.  Predicting the viability of beta-lactamase: How folding and binding free energies correlate with beta-lactamase fitness.. PLoS One. 15(5):e0233509.
2017
Gapsys V, de Groot BL.  2017.  Alchemical Free Energy Calculations for Nucleotide Mutations in Protein-DNA Complexes.. J Chem Theory Comput. 13(12):6275-6289.
Nosrati M, Solbak S, Nordesjö O, Nissbeck M, Dourado DFAR, Andersson KG, Housaindokht MReza, Löfblom J, Virtanen A, U Danielson H et al..  2017.  Insights from engineering the Affibody-Fc interaction with a computational-experimental method.. Protein Eng Des Sel. 30(9):593-601.
2016
Sirin S, Apgar JR, Bennett EM, Keating AE.  2016.  AB-Bind: Antibody binding mutational database for computational affinity predictions.. Protein Sci. 25(2):393-409.
Sulea T, Vivcharuk V, Corbeil CR, Deprez C, Purisima EO.  2016.  Assessment of Solvated Interaction Energy Function for Ranking Antibody-Antigen Binding Affinities.. J Chem Inf Model. 56(7):1292-303.
Huwe PJ, Xu Q, Shapovalov MV, Modi V, Andrake MD, Dunbrack RL.  2016.  Biological function derived from predicted structures in CASP11.. Proteins. 84 Suppl 1:370-91.
Kowalsky CA, Whitehead TA.  2016.  Determination of binding affinity upon mutation for type I dockerin-cohesin complexes from Clostridium thermocellum and Clostridium cellulolyticum using deep sequencing.. Proteins. 84(12):1914-1928.
Tomar JSingh, Peddinti RKrishna.  2016.  Optimized method for TAG protein homology modeling: In silico and experimental structural characterization.. Int J Biol Macromol. 88:102-12.
Van Durme J, De Baets G, Van Der Kant R, Ramakers M, Ganesan A, Wilkinson H, Gallardo R, Rousseau F, Schymkowitz J.  2016.  Solubis: a webserver to reduce protein aggregation through mutation.. Protein Eng Des Sel. 29(8):285-9.
2014
Liu Q, Hoi SCH, Kwoh CKeong, Wong L, Li J.  2014.  Integrating water exclusion theory into β contacts to predict binding free energy changes and binding hot spots.. BMC Bioinformatics. 15:57.
2007
Pey AL, Stricher F, Serrano L, Martinez A.  2007.  Predicted effects of missense mutations on native-state stability account for phenotypic outcome in phenylketonuria, a paradigm of misfolding diseases.. Am J Hum Genet. 81(5):1006-24.
2005
Wohlgemuth S, Kiel C, Krämer A, Serrano L, Wittinghofer F, Herrmann C.  2005.  Recognizing and defining true Ras binding domains I: biochemical analysis.. J Mol Biol. 348(3):741-58.
Kiel C, Wohlgemuth S, Rousseau F, Schymkowitz J, Ferkinghoff-Borg J, Wittinghofer F, Serrano L.  2005.  Recognizing and defining true Ras binding domains II: in silico prediction based on homology modelling and energy calculations.. J Mol Biol. 348(3):759-75.
2004
Kiel C, Serrano L, Herrmann C.  2004.  A detailed thermodynamic analysis of ras/effector complex interfaces.. J Mol Biol. 340(5):1039-58.
2002
Guerois R, Nielsen J E, Serrano L.  2002.  Predicting changes in the stability of proteins and protein complexes: a study of more than 1000 mutations.. J Mol Biol. 320(2):369-87.
1999
Petukhov M, Cregut D, Soares CM, Serrano L.  1999.  Local water bridges and protein conformational stability.. Protein Sci. 8(10):1982-9.
1994
Abagyan R, Totrov M.  1994.  Biased probability Monte Carlo conformational searches and electrostatic calculations for peptides and proteins.. J Mol Biol. 235(3):983-1002.
Muñoz V, Serrano L.  1994.  Intrinsic secondary structure propensities of the amino acids, using statistical phi-psi matrices: comparison with experimental scales.. Proteins. 20(4):301-11.