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Showing results (141-150 of 224) with videos related to

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Biochemistry|January 19, 1993
Comparison of backbone and tryptophan side-chain dynamics of reduced and oxidized Escherichia coli thioredoxin using 15N NMR relaxation measurementsM J Stone, K Chandrasekhar, A Holmgren, et al.
Biochemistry|April 29, 1997
Contribution of increased length and intact capping sequences to the conformational preference for helix in a 31-residue peptide from the C terminus of myohemerythrinM T Reymond, S Huo, B Duggan, et al.
FEBS Letters|January 30, 1992
Low resolution solution structure of the Bacillus subtilis glucose permease IIA domain derived from heteronuclear three-dimensional NMR spectroscopyW J Fairbrother, G P Gippert, J Reizer, et al.
Journal of Molecular Biology|August 5, 1992
Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. I. MyohemerythrinH J Dyson, G Merutka, J P Waltho, et al.
Peptide Research|November 1, 1988
Isotope-edited NMR studies of Fab'-peptide complexesP Tsang, T M Fieser, J M Ostresh, et al.
Biochemistry|June 29, 1993
Peptide models of protein folding initiation sites. 1. Secondary structure formation by peptides corresponding to the G- and H-helices of myoglobinJ P Waltho, V A Feher, G Merutka, et al.
Biochemistry|August 15, 2001
Backbone dynamics in dihydrofolate reductase complexes: role of loop flexibility in the catalytic mechanismM J Osborne, J Schnell, S J Benkovic, et al.
Biochemistry|June 29, 1993
Peptide models of protein folding initiation sites. 2. The G-H turn region of myoglobin acts as a helix stop signalH C Shin, G Merutka, J P Waltho, et al.
Protein Science : a Publication of the Protein Society|April 21, 1999
Quench-flow experiments combined with mass spectrometry show apomyoglobin folds through and obligatory intermediateV Tsui, C Garcia, S Cavagnero, et al.
Science (New York, N.Y.)|May 21, 1993
Structure of the retinoid X receptor alpha DNA binding domain: a helix required for homodimeric DNA bindingM S Lee, S A Kliewer, J Provencal, et al.
Pageof 23

Showing results (141-150 of 224) with videos related to

Sort By:
Pageof 23
Biochemistry|January 19, 1993
Comparison of backbone and tryptophan side-chain dynamics of reduced and oxidized Escherichia coli thioredoxin using 15N NMR relaxation measurementsM J Stone, K Chandrasekhar, A Holmgren, et al.
Biochemistry|April 29, 1997
Contribution of increased length and intact capping sequences to the conformational preference for helix in a 31-residue peptide from the C terminus of myohemerythrinM T Reymond, S Huo, B Duggan, et al.
FEBS Letters|January 30, 1992
Low resolution solution structure of the Bacillus subtilis glucose permease IIA domain derived from heteronuclear three-dimensional NMR spectroscopyW J Fairbrother, G P Gippert, J Reizer, et al.
Journal of Molecular Biology|August 5, 1992
Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. I. MyohemerythrinH J Dyson, G Merutka, J P Waltho, et al.
Peptide Research|November 1, 1988
Isotope-edited NMR studies of Fab'-peptide complexesP Tsang, T M Fieser, J M Ostresh, et al.
Biochemistry|June 29, 1993
Peptide models of protein folding initiation sites. 1. Secondary structure formation by peptides corresponding to the G- and H-helices of myoglobinJ P Waltho, V A Feher, G Merutka, et al.
Biochemistry|August 15, 2001
Backbone dynamics in dihydrofolate reductase complexes: role of loop flexibility in the catalytic mechanismM J Osborne, J Schnell, S J Benkovic, et al.
Biochemistry|June 29, 1993
Peptide models of protein folding initiation sites. 2. The G-H turn region of myoglobin acts as a helix stop signalH C Shin, G Merutka, J P Waltho, et al.
Protein Science : a Publication of the Protein Society|April 21, 1999
Quench-flow experiments combined with mass spectrometry show apomyoglobin folds through and obligatory intermediateV Tsui, C Garcia, S Cavagnero, et al.
Science (New York, N.Y.)|May 21, 1993
Structure of the retinoid X receptor alpha DNA binding domain: a helix required for homodimeric DNA bindingM S Lee, S A Kliewer, J Provencal, et al.
Pageof 23