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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.

Nucleic Acids Research|July 1, 1996

Assessment of major and minor groove DNA interactions by the zinc fingers of Xenopus transcription factor IIIAS J McBryant, B Gedulin, K R Clemens, et al.

Journal of Molecular Biology|May 5, 1988

Folding of immunogenic peptide fragments of proteins in water solution. II. The nascent helixH J Dyson, M Rance, R A Houghten, et al.

Journal of Molecular Biology|August 17, 1999

Identification of a minimal domain of 5 S ribosomal RNA sufficient for high affinity interactions with the RNA-specific zinc fingers of transcription factor IIIAL S Neely, B M Lee, J Xu, et al.

Journal of Molecular Biology|July 13, 2000

Solution structure of the cysteine-rich domain of the Escherichia coli chaperone protein DnaJM Martinez-Yamout, G B Legge, O Zhang, et al.

The Biochemical Journal|September 1, 1995

Recombinant soluble human tissue factor secreted by Saccharomyces cerevisiae and refolded from Escherichia coli inclusion bodies: glycosylation of mutants, activity and physical characterizationM J Stone, W Ruf, D J Miles, et al.

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Showing results (151-160 of 223) with videos related to

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Pageof 23

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.

Nucleic Acids Research|July 1, 1996

Assessment of major and minor groove DNA interactions by the zinc fingers of Xenopus transcription factor IIIAS J McBryant, B Gedulin, K R Clemens, et al.

Journal of Molecular Biology|May 5, 1988

Folding of immunogenic peptide fragments of proteins in water solution. II. The nascent helixH J Dyson, M Rance, R A Houghten, et al.

Journal of Molecular Biology|August 17, 1999

Identification of a minimal domain of 5 S ribosomal RNA sufficient for high affinity interactions with the RNA-specific zinc fingers of transcription factor IIIAL S Neely, B M Lee, J Xu, et al.

Journal of Molecular Biology|July 13, 2000

Solution structure of the cysteine-rich domain of the Escherichia coli chaperone protein DnaJM Martinez-Yamout, G B Legge, O Zhang, et al.

The Biochemical Journal|September 1, 1995

Recombinant soluble human tissue factor secreted by Saccharomyces cerevisiae and refolded from Escherichia coli inclusion bodies: glycosylation of mutants, activity and physical characterizationM J Stone, W Ruf, D J Miles, et al.

Pageof 23