Skip NavigationSkip to Content

NCI at Frederick Scientific Publications Advanced Search

Search

  1. NCI-F Publications

  2. Return to Quick Search
Search
  2. Year Published:

Your search returned 17 results.
User Information
Export Records
  1. 1.   Constructing templates for protein structure prediction by simulation of protein folding pathways
  2. Kifer, I.; Nussinov, R.; Wolfson, H. J.
  3. Proteins-Structure Function and Bioinformatics. 2008 73(2): 380-394.
  1. 2.   How different are structurally flexible and rigid binding sites? Sequence and structural features discriminating proteins that do and do not undergo conformational change upon ligand binding
  2. Gunasekaran, K.; Nussinov, R.
  3. Journal of Molecular Biology. 2007, Jan; 365(1): 257-273.
  1. 3.   Combinatorial docking approach for structure prediction of large proteins and multi-molecular assemblies
  2. Inbar, Y.; Benyamini, H.; Nussinov, R.; Wolfson, H. J.
  3. Physical Biology. 2005, DEC; 2(4, Sp. Iss.): S156-S165.
  1. 4.   Prediction of multimolecular assemblies by multiple docking
  2. Inbar, Y.; Benyamini, H.; Nussinov, R.; Wolfson, H. J.
  3. Journal of Molecular Biology. 2005, JUN 3; 349(2): 435-447.
  1. 5.   Multiple docking for protein structure prediction
  2. Inbar, Y.; Wolfson, H. J.; Nussinov, R.
  3. International Journal of Robotics Research. 2005, FEB-MAR; 24(2-3): 131-150.
  1. 6.   In silico protein design by combinatorial assembly of protein building blocks
  2. Tsai, H. H.; Tsai, C. J.; Ma, B. Y.; Nussinov, R.
  3. Protein Science. 2004, OCT; 13(10): 2753-2765.
  1. 7.   Hierarchical protein folding pathways: A computational study of protein fragments
  2. Haspel, N.; Tsai, C. J.; Wolfson, H.; Nussinov, R.
  3. Proteins-Structure Function and Genetics. 2003 51(2): 203-215.
  1. 8.   Thermodynamic differences among homologous thermophilic and mesophilic proteins
  2. Kumar, S.; Tsai, C. J.; Nussinov, R.
  3. Biochemistry. 2001 40(47): 14152-14165.
  1. 9.   Interdomain interactions in hinge-bending transitions
  2. Sinha, N.; Kumar, S.; Nussinov, R.
  3. Structure. 2001 9(12): 1165-1181.
  1. 10.   A systematic study of the vibrational free energies of polypeptides in folded and random states
  2. Ma, B. Y.; Tsai, C. J.; Nussinov, R.
  3. Biophysical Journal. 2000 79(5): 2739-2753.
  1. 11.   Logos for amino-acid preferences in different backbone packing density regions of protein structural classes
  2. Kannan, N.; Schneider, T. D.; Vishveshwara, S.
  3. Acta Crystallographica Section D-Biological Crystallography. 2000 56(Part 9): 1156-1165.
  1. 12.   Factors enhancing protein thermostability
  2. Kumar, S.; Tsai, C. J.; Nussinov, R.
  3. Protein Engineering. 2000 13(3): 179-191.
  1. 13.   Molecular mechanisms of resistance: Free energy calculations of mutation effects on inhibitor binding to HIV-1 protease
  2. Rick, S. W.; Topol, I. A.; Erickson, J. W.; Burt, S. K.
  3. Protein Science. 1998 7(8): 1750-1756.
  1. 14.   Protein Folding Via Binding and Vice Versa
  2. Tsai, C. J.; Xu, D.; Nussinov, R.
  3. Folding and Design. 1998 3(4): R 71-R 80.
  1. 15.   Hydrophobic Folding Units At Protein-Protein Interfaces - Implications to Protein Folding and to Protein-Protein Association
  2. Tsai, C. J.; Nussinov, R.
  3. Protein Science. 1997 6(7): 1426-1437.
  1. 16.   Structural Motifs At Protein-Protein Interfaces - Protein Cores Versus Two-State and Three-State Model Complexes
  2. Tsai, C. J.; Xu, D.; Nussinov, R.
  3. Protein Science. 1997 6(9): 1793-1805.
  1. 17.   Hydrophobic Folding Units Derived From Dissimilar Monomer Structures and Their Interactions
  2. Tsai, C. J.; Nussinov, R.
  3. Protein Science. 1997 6(1): 24-42.
NCI at Frederick

You are leaving a government website.

This external link provides additional information that is consistent with the intended purpose of this site. The government cannot attest to the accuracy of a non-federal site.

Linking to a non-federal site does not constitute an endorsement by this institution or any of its employees of the sponsors or the information and products presented on the site. You will be subject to the destination site's privacy policy when you follow the link.

ContinueCancel