Research Topics
| Suparna Chandra SanyalSummaryAffiliation: Lund University Country: Sweden Publications
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Detail Information
Publications
23S rRNA assisted folding of cytoplasmic malate dehydrogenase is distinctly different from its self-foldingSuparna Chandra Sanyal
Department of Biophysics, Molecular Biology and Genetics, University College of Science, University of Calcutta, 92 A P C Road, Kolkata 700 009, India
Nucleic Acids Res 30:2390-7. 2002....
The end of the beginning: structural studies of ribosomal proteinsS Chandra Sanyal
Molecular Biophysics, Lund University, Box 124, SE 221 00, Lund, Sweden
Curr Opin Struct Biol 10:633-6. 2000..The structure provides a missing link for many previous biochemical and functional studies...
Crystal structure of Thermotoga maritima ribosome recycling factor: a tRNA mimicM Selmer
Molecular Biophysics, Center for Chemistry and Chemical Engineering, Lund University, Post Office Box 124, SE 22100 Lund, Sweden
Science 286:2349-52. 1999..The structural arrangement of this mimicry is entirely different from that of other cases of less pronounced mimicry of tRNA so far described...
Crystal structure of a superantigen bound to MHC class II displays zinc and peptide dependenceK Petersson
Molecular Biophysics, Centre for Chemistry and Chemical Engineering, Lund University, PO Box 124, S 221 00 Lund, Sweden
EMBO J 20:3306-12. 2001..This suggests a new model for ternary complex formation with the T-cell receptor (TCR), in which a contact between the TCR and the MHC class II is unlikely...
A decade of progress in understanding the structural basis of protein synthesisS Al-Karadaghi
Department of Molecular Biophysics, Lund University, Box 124, 221 00, Lund, Sweden
Prog Biophys Mol Biol 73:167-93. 2000..The new structural data have opened a way for the design of new experiments aimed at deeper understanding at an atomic level of the dynamics of the system...
Crystallization and preliminary X-ray analysis of Thermotoga maritima ribosome recycling factorM Selmer
Department of Molecular Biophysics, Center for Chemistry and Chemical Engineering, Lund University, Box 124, 22100 Lund, Sweden
Acta Crystallogr D Biol Crystallogr 55:2049-50. 1999..The crystals belong to space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = b = 47, c = 298 A, and probably contain one monomer per asymmetric unit...
The crystal structure of ribosomal protein L22 from Thermus thermophilus: insights into the mechanism of erythromycin resistanceJ Unge
Molecular Biophysics, Lund University, PO Box 124 221 00 Lund, Sweden
Structure 6:1577-86. 1998..Knowing the structure of the protein may resolve this apparent conflict regarding the location of L22 on the ribosome...
A ribosomal protein from Thermus thermophilus is homologous to a general shock proteinO I Gryaznova
Center of Chemistry and Chemical Engineering, Lund University, Sweden
Biochimie 78:915-9. 1996..The evolutionary relationship of a heat shock protein in mesophiles and a ribosomal protein in thermophilic bacteria as well as a possible role of TL5 in the ribosome are discussed...
Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding siteM Laurberg
Department of Molecular Biophysics, Centre for Chemistry and Chemical Engineering, Lund University, Lund, SE 221 00, Sweden
J Mol Biol 303:593-603. 2000..Possible locations for the effector loop and a possible binding site for fusidic acid are discussed in relation to some of the fusidic acid resistant mutations...
The structure of elongation factor G in complex with GDP: conformational flexibility and nucleotide exchangeS Al-Karadaghi
Department of Molecular Biophysics, Lund University, Sweden
Structure 4:555-65. 1996..The first two of these conformations have been previously investigated by crystallographic methods...
Imprinting through molecular mimicry. Protein synthesisA Liljas
Molecular Biophysics, Center for Chemistry and Chemical Engineering, Lund University, Box 124, S 221 00 Lund, Sweden
Curr Biol 6:247-9. 1996..Part of the structure of translational elongation factor G, in a complex with GDP, resembles the tRNA bound in a ternary complex with elongation factor Tu and GTP; this 'molecular mimicry' extends to charge distribution as well as shape...
Ribosomal protein L22 from Thermus thermophilus: sequencing, overexpression and crystallisationN L Davydova
Molecular Biophysics, University of Lund, Sweden
FEBS Lett 369:229-32. 1995..The recombinant protein was purified and crystallized. The crystals belong to the space group P2(1)2(1)2(1), with cell parameters of a = 32.6 A, b = 66.0 A, c = 67.8 A...
