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444 related items for PubMed ID: 8976569
1. Conformational analysis and clustering of short and medium size loops connecting regular secondary structures: a database for modeling and prediction. Donate LE, Rufino SD, Canard LH, Blundell TL. Protein Sci; 1996 Dec; 5(12):2600-16. PubMed ID: 8976569 [Abstract] [Full Text] [Related]
2. Analysis, clustering and prediction of the conformation of short and medium size loops connecting regular secondary structures. Rufino SD, Donate LE, Canard L, Blundell TL. Pac Symp Biocomput; 1996 Dec; ():570-89. PubMed ID: 9390259 [Abstract] [Full Text] [Related]
6. An automated classification of the structure of protein loops. Oliva B, Bates PA, Querol E, Avilés FX, Sternberg MJ. J Mol Biol; 1997 Mar 07; 266(4):814-30. PubMed ID: 9102471 [Abstract] [Full Text] [Related]
8. Fragment ranking in modelling of protein structure. Conformationally constrained environmental amino acid substitution tables. Topham CM, McLeod A, Eisenmenger F, Overington JP, Johnson MS, Blundell TL. J Mol Biol; 1993 Jan 05; 229(1):194-220. PubMed ID: 8421300 [Abstract] [Full Text] [Related]
9. Prediction of the conformation and geometry of loops in globular proteins: testing ArchDB, a structural classification of loops. Fernandez-Fuentes N, Querol E, Aviles FX, Sternberg MJ, Oliva B. Proteins; 2005 Sep 01; 60(4):746-57. PubMed ID: 16021623 [Abstract] [Full Text] [Related]
10. [A turning point in the knowledge of the structure-function-activity relations of elastin]. Alix AJ. J Soc Biol; 2001 Sep 01; 195(2):181-93. PubMed ID: 11727705 [Abstract] [Full Text] [Related]
11. Conformations of the third hypervariable region in the VH domain of immunoglobulins. Morea V, Tramontano A, Rustici M, Chothia C, Lesk AM. J Mol Biol; 1998 Jan 16; 275(2):269-94. PubMed ID: 9466909 [Abstract] [Full Text] [Related]
12. Modeling protein loops using a phi i + 1, psi i dimer database. Sudarsanam S, DuBose RF, March CJ, Srinivasan S. Protein Sci; 1995 Jul 16; 4(7):1412-20. PubMed ID: 7670382 [Abstract] [Full Text] [Related]
13. Automatic classification and analysis of alpha alpha-turn motifs in proteins. Wintjens RT, Rooman MJ, Wodak SJ. J Mol Biol; 1996 Jan 12; 255(1):235-53. PubMed ID: 8568871 [Abstract] [Full Text] [Related]
14. The energy of formation of internal loops in triple-helical collagen polypeptides. Paterlini MG, Némethy G, Scheraga HA. Biopolymers; 1995 Jun 12; 35(6):607-19. PubMed ID: 7766826 [Abstract] [Full Text] [Related]
15. Linkers of secondary structures in proteins. Geetha V, Munson PJ. Protein Sci; 1997 Dec 12; 6(12):2538-47. PubMed ID: 9416603 [Abstract] [Full Text] [Related]
16. Expanded turn conformations: characterization and sequence-structure correspondence in alpha-turns with implications in helix folding. Dasgupta B, Pal L, Basu G, Chakrabarti P. Proteins; 2004 May 01; 55(2):305-15. PubMed ID: 15048823 [Abstract] [Full Text] [Related]
17. The identification of conserved interactions within the SH3 domain by alignment of sequences and structures. Larson SM, Davidson AR. Protein Sci; 2000 Nov 01; 9(11):2170-80. PubMed ID: 11152127 [Abstract] [Full Text] [Related]
18. The nature of the turn in omega loops of proteins. Pal M, Dasgupta S. Proteins; 2003 Jun 01; 51(4):591-606. PubMed ID: 12784218 [Abstract] [Full Text] [Related]
19. GlnK, a PII-homologue: structure reveals ATP binding site and indicates how the T-loops may be involved in molecular recognition. Xu Y, Cheah E, Carr PD, van Heeswijk WC, Westerhoff HV, Vasudevan SG, Ollis DL. J Mol Biol; 1998 Sep 11; 282(1):149-65. PubMed ID: 9733647 [Abstract] [Full Text] [Related]
20. Conformational interconversions in peptide beta-turns: analysis of turns in proteins and computational estimates of barriers. Gunasekaran K, Gomathi L, Ramakrishnan C, Chandrasekhar J, Balaram P. J Mol Biol; 1998 Dec 18; 284(5):1505-16. PubMed ID: 9878367 [Abstract] [Full Text] [Related] Page: [Next] [New Search]