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The interrelationships of side-chain and main-chain conformations in proteins.
Chakrabarti P, Pal D. Chakrabarti P, et al. Among authors: pal d. Prog Biophys Mol Biol. 2001;76(1-2):1-102. doi: 10.1016/s0079-6107(01)00005-0. Prog Biophys Mol Biol. 2001. PMID: 11389934 Review.
beta-sheet propensity and its correlation with parameters based on conformation.
Pal D, Chakrabarti P. Pal D, et al. Acta Crystallogr D Biol Crystallogr. 2000 May;56(Pt 5):589-94. doi: 10.1107/s090744490000367x. Acta Crystallogr D Biol Crystallogr. 2000. PMID: 10771428
The dispersion of the main-chain and side-chain conformations in the phi, psi, chi(1) space for all residues have been estimated in terms of three parameters corresponding to the entropy (S) of the distribution, the volume (D(V)) and the area (D(A)) the points are e …
The dispersion of the main-chain and side-chain conformations in the phi, psi, chi(1) space for all residues have been estimated in terms of …
Packing of aromatic rings against tryptophan residues in proteins.
Samanta U, Pal D, Chakrabarti P. Samanta U, et al. Among authors: pal d. Acta Crystallogr D Biol Crystallogr. 1999 Aug;55(Pt 8):1421-7. doi: 10.1107/s090744499900726x. Acta Crystallogr D Biol Crystallogr. 1999. PMID: 10417410
Conformational properties of alpha-tubulin tail peptide: implications for tail-body interaction.
Pal D, Mahapatra P, Manna T, Chakrabarti P, Bhattacharyya B, Banerjee A, Basu G, Roy S. Pal D, et al. Biochemistry. 2001 Dec 25;40(51):15512-9. doi: 10.1021/bi015677t. Biochemistry. 2001. PMID: 11747426
Non-hydrogen bond interactions involving the methionine sulfur atom.
Pal D, Chakrabarti P. Pal D, et al. J Biomol Struct Dyn. 2001 Aug;19(1):115-28. doi: 10.1080/07391102.2001.10506725. J Biomol Struct Dyn. 2001. PMID: 11565843
Conformational similarity indices between different residues in proteins and alpha-helix propensities.
Pal D, Chakrabarti P. Pal D, et al. J Biomol Struct Dyn. 2000 Oct;18(2):273-80. doi: 10.1080/07391102.2000.10506665. J Biomol Struct Dyn. 2000. PMID: 11089648
Terminal residues in protein chains: residue preference, conformation, and interaction.
Pal D, Chakrabarti P. Pal D, et al. Biopolymers. 2000 May;53(6):467-75. doi: 10.1002/(SICI)1097-0282(200005)53:6<467::AID-BIP3>3.0.CO;2-9. Biopolymers. 2000. PMID: 10775062
Environment of tryptophan side chains in proteins.
Samanta U, Pal D, Chakrabarti P. Samanta U, et al. Among authors: pal d. Proteins. 2000 Feb 15;38(3):288-300. Proteins. 2000. PMID: 10713989
Cis peptide bonds in proteins: residues involved, their conformations, interactions and locations.
Pal D, Chakrabarti P. Pal D, et al. J Mol Biol. 1999 Nov 19;294(1):271-88. doi: 10.1006/jmbi.1999.3217. J Mol Biol. 1999. PMID: 10556045
Graphical representation of the salient conformational features of protein residues.
Pal D, Chakrabarti P. Pal D, et al. Protein Eng. 1999 Jul;12(7):523-6. doi: 10.1093/protein/12.7.523. Protein Eng. 1999. PMID: 10436077
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