Suparna Chandra Sanyal
Affiliation: Lund University
- 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...