D E Tronrud|S L Roderick|B W Matthews - JoVE Visualize

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Biochemistry|January 13, 1987

Comparison of the precursor and mature forms of rat heart mitochondrial malate dehydrogenaseP M Grant, S L Roderick, G A Grant, et al.

Protein Engineering|October 1, 1995

Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additiveX J Zhang, W A Baase, B K Shoichet, et al.

Protein Engineering|June 2, 2000

Use of a non-rigid region in T4 lysozyme to design an adaptable metal-binding siteJ W Wray, W A Baase, G J Ostheimer, et al.

Proceedings of the National Academy of Sciences of the United States of America|May 1, 1982

Structural similarity in the DNA-binding domains of catabolite gene activator and cro repressor proteinsT A Steitz, D H Ohlendorf, D B McKay, et al.

Biochemistry|October 26, 1993

Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozymeM Blaber, J D Lindstrom, N Gassner, et al.

Journal of Molecular Biology|September 20, 1987

Structural studies of mutants of the lysozyme of bacteriophage T4. The temperature-sensitive mutant protein Thr157----IleM G Grütter, T M Gray, L H Weaver, et al.

Nature|May 3, 1990

Ancestral lysozymes reconstructed, neutrality tested, and thermostability linked to hydrocarbon packingB A Malcolm, K P Wilson, B W Matthews, et al.

Proceedings of the National Academy of Sciences of the United States of America|October 1, 1992

Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domainsK P Wilson, L M Shewchuk, R G Brennan, et al.

Biochemistry|December 10, 1991

Structural and thermodynamic consequences of burying a charged residue within the hydrophobic core of T4 lysozymeS Dao-pin, D E Anderson, W A Baase, et al.

Proceedings of the National Academy of Sciences of the United States of America|August 15, 1993

Amino acid residues essential for biological activity of a peptide derived from a major histocompatibility complex class I antigenJ Stagsted, C Mapelli, C Meyers, et al.

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Showing results (161-170 of 193) with videos related to

Sort By:

Pageof 20

Biochemistry|January 13, 1987

Comparison of the precursor and mature forms of rat heart mitochondrial malate dehydrogenaseP M Grant, S L Roderick, G A Grant, et al.

Protein Engineering|October 1, 1995

Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additiveX J Zhang, W A Baase, B K Shoichet, et al.

Protein Engineering|June 2, 2000

Use of a non-rigid region in T4 lysozyme to design an adaptable metal-binding siteJ W Wray, W A Baase, G J Ostheimer, et al.

Proceedings of the National Academy of Sciences of the United States of America|May 1, 1982

Structural similarity in the DNA-binding domains of catabolite gene activator and cro repressor proteinsT A Steitz, D H Ohlendorf, D B McKay, et al.

Biochemistry|October 26, 1993

Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozymeM Blaber, J D Lindstrom, N Gassner, et al.

Journal of Molecular Biology|September 20, 1987

Structural studies of mutants of the lysozyme of bacteriophage T4. The temperature-sensitive mutant protein Thr157----IleM G Grütter, T M Gray, L H Weaver, et al.

Nature|May 3, 1990

Ancestral lysozymes reconstructed, neutrality tested, and thermostability linked to hydrocarbon packingB A Malcolm, K P Wilson, B W Matthews, et al.

Proceedings of the National Academy of Sciences of the United States of America|October 1, 1992

Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domainsK P Wilson, L M Shewchuk, R G Brennan, et al.

Biochemistry|December 10, 1991

Structural and thermodynamic consequences of burying a charged residue within the hydrophobic core of T4 lysozymeS Dao-pin, D E Anderson, W A Baase, et al.

Proceedings of the National Academy of Sciences of the United States of America|August 15, 1993

Amino acid residues essential for biological activity of a peptide derived from a major histocompatibility complex class I antigenJ Stagsted, C Mapelli, C Meyers, et al.

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