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M F Perutz

Showing results (111-120 of 138) with videos related to

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Proceedings of the National Academy of Sciences of the United States of America|May 15, 1991
The rhombotin family of cysteine-rich LIM-domain oncogenes: distinct members are involved in T-cell translocations to human chromosomes 11p15 and 11p13T Boehm, L Foroni, Y Kaneko, et al.
Biochemistry|May 7, 1974
Influence of globin structure on the state of the heme. II. Allosteric transitions in methemoglobinM F Perutz, A R Fersht, S R Simon, et al.
Proceedings of the National Academy of Sciences of the United States of America|January 1, 1972
Noncooperativity of the dimer in the reaction of hemoglobin with oxygen (human-dissociation-equilibrium-sulfhydryl-absorption-x-ray analysis)J A Hewitt, J V Kilmartin, L F Eyck, et al.
Biochemistry|January 27, 1976
Influence of globin structures on the state of the heme. Ferrous low spin derivativesM F Perutz, J V Kilmartin, K Nagai, et al.
Proceedings of the National Academy of Sciences of the United States of America|April 18, 2002
Aggregation of proteins with expanded glutamine and alanine repeats of the glutamine-rich and asparagine-rich domains of Sup35 and of the amyloid beta-peptide of amyloid plaquesM F Perutz, B J Pope, D Owen, et al.
Proceedings of the National Academy of Sciences of the United States of America|February 15, 1994
Formation of two hydrogen bonds from the globin to the heme-linked oxygen molecule in Ascaris hemoglobinI De Baere, M F Perutz, L Kiger, et al.
The Journal of Biological Chemistry|January 5, 1990
Hemoglobin Warsaw (Phe beta 42(CD1)----Val), an unstable variant with decreased oxygen affinity. Characterization of its synthesis, functional properties, and structureG R Honig, L N Vida, B B Rosenblum, et al.
The Journal of Biological Chemistry|July 5, 1989
Structure and function of human hemoglobin covalently labeled with periodate-oxidized adenosine triphosphateM P Kavanaugh, M F Perutz, G Fermi, et al.
Proceedings of the National Academy of Sciences of the United States of America|March 1, 1978
Structure of hemoglobins Zürich [His E7(63)beta replaced by Arg] and Sydney [Val E11(67)beta replaced by Ala] and role of the distal residues in ligand bindingP W Tucker, S E Phillips, M F Perutz, et al.
Journal of Molecular Biology|June 5, 1985
The pKa values of two histidine residues in human haemoglobin, the Bohr effect, and the dipole moments of alpha-helicesM F Perutz, A M Gronenborn, G M Clore, et al.
Pageof 14

Showing results (111-120 of 138) with videos related to

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Pageof 14
Proceedings of the National Academy of Sciences of the United States of America|May 15, 1991
The rhombotin family of cysteine-rich LIM-domain oncogenes: distinct members are involved in T-cell translocations to human chromosomes 11p15 and 11p13T Boehm, L Foroni, Y Kaneko, et al.
Biochemistry|May 7, 1974
Influence of globin structure on the state of the heme. II. Allosteric transitions in methemoglobinM F Perutz, A R Fersht, S R Simon, et al.
Proceedings of the National Academy of Sciences of the United States of America|January 1, 1972
Noncooperativity of the dimer in the reaction of hemoglobin with oxygen (human-dissociation-equilibrium-sulfhydryl-absorption-x-ray analysis)J A Hewitt, J V Kilmartin, L F Eyck, et al.
Biochemistry|January 27, 1976
Influence of globin structures on the state of the heme. Ferrous low spin derivativesM F Perutz, J V Kilmartin, K Nagai, et al.
Proceedings of the National Academy of Sciences of the United States of America|April 18, 2002
Aggregation of proteins with expanded glutamine and alanine repeats of the glutamine-rich and asparagine-rich domains of Sup35 and of the amyloid beta-peptide of amyloid plaquesM F Perutz, B J Pope, D Owen, et al.
Proceedings of the National Academy of Sciences of the United States of America|February 15, 1994
Formation of two hydrogen bonds from the globin to the heme-linked oxygen molecule in Ascaris hemoglobinI De Baere, M F Perutz, L Kiger, et al.
The Journal of Biological Chemistry|January 5, 1990
Hemoglobin Warsaw (Phe beta 42(CD1)----Val), an unstable variant with decreased oxygen affinity. Characterization of its synthesis, functional properties, and structureG R Honig, L N Vida, B B Rosenblum, et al.
The Journal of Biological Chemistry|July 5, 1989
Structure and function of human hemoglobin covalently labeled with periodate-oxidized adenosine triphosphateM P Kavanaugh, M F Perutz, G Fermi, et al.
Proceedings of the National Academy of Sciences of the United States of America|March 1, 1978
Structure of hemoglobins Zürich [His E7(63)beta replaced by Arg] and Sydney [Val E11(67)beta replaced by Ala] and role of the distal residues in ligand bindingP W Tucker, S E Phillips, M F Perutz, et al.
Journal of Molecular Biology|June 5, 1985
The pKa values of two histidine residues in human haemoglobin, the Bohr effect, and the dipole moments of alpha-helicesM F Perutz, A M Gronenborn, G M Clore, et al.
Pageof 14