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Nature|August 31, 1995
Structural basis for DNA bending by the architectural transcription factor LEF-1J J Love, X Li, D A Case, et al.Biochemistry|May 22, 1992
Assignment of the aliphatic 1H and 13C resonances of the Bacillus subtilis glucose permease IIA domain using double- and triple-resonance heteronuclear three-dimensional NMR spectroscopyW J Fairbrother, A G Palmer, M Rance, et al.Journal of Biomolecular NMR|July 1, 1994
1H and 15N resonance assignments and secondary structure of the carbon monoxide complex of sperm whale myoglobinY Thériault, T C Pochapsky, C Dalvit, et al.Journal of the American Chemical Society|July 18, 2001
Sequence-dependent correction of random coil NMR chemical shiftsS Schwarzinger, G J Kroon, T R Foss, et al.Journal of Molecular Biology|October 12, 2000
Solution structure of the TAZ2 (CH3) domain of the transcriptional adaptor protein CBPR N De Guzman, H Y Liu, M Martinez-Yamout, et al.Journal of Molecular Biology|November 18, 1994
Relative contributions of the zinc fingers of transcription factor IIIA to the energetics of DNA bindingK R Clemens, P Zhang, X Liao, et al.European Journal of Biochemistry|August 26, 1998
Sequence requirements for stabilization of a peptide reverse turn in water solution--proline is not essential for stabilityH J Dyson, L Bolinger, V A Feher, et al.Biochemistry|February 11, 1992
Immunogenic peptides corresponding to the dominant antigenic region alanine-597 to cysteine-619 in the transmembrane protein of simian immunodeficiency virus have a propensity to fold in aqueous solutionH J Dyson, E Norrby, K Hoey, et al.Journal of Molecular Biology|November 4, 1994
Stabilization of a type VI turn in a family of linear peptides in water solutionJ Yao, V A Feher, B F Espejo, et al.Biochemistry|June 29, 1993
Peptide models of protein folding initiation sites. 3. The G-H helical hairpin of myoglobinH C Shin, G Merutka, J P Waltho, et al.Pageof 23