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C Altenbach

Showing results (21-30 of 37) with videos related to

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Biochemistry|December 19, 2001
Structure and function in rhodopsin: mapping light-dependent changes in distance between residue 316 in helix 8 and residues in the sequence 60-75, covering the cytoplasmic end of helices TM1 and TM2 and their connection loop CL1C Altenbach, J Klein-Seetharaman, K Cai, et al.
Science (New York, N.Y.)|November 1, 1996
Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsinD L Farrens, C Altenbach, K Yang, et al.
Biochemistry|September 14, 2000
Binding of spin-labeled galactosides to the lactose permease of Escherichia coliM Zhao, T Kálai, K Hideg, et al.
Biochemistry|August 11, 1999
Conformation of the diphtheria toxin T domain in membranes: a site-directed spin-labeling study of the TH8 helix and TL5 loopK J Oh, H Zhan, C Cui, et al.
Biochemistry|October 17, 2001
Probing the dark state tertiary structure in the cytoplasmic domain of rhodopsin: proximities between amino acids deduced from spontaneous disulfide bond formation between Cys316 and engineered cysteines in cytoplasmic loop 1J Klein-Seetharaman, J Hwa, K Cai, et al.
Biochemistry|July 1, 1999
Single-cysteine substitution mutants at amino acid positions 55-75, the sequence connecting the cytoplasmic ends of helices I and II in rhodopsin: reactivity of the sulfhydryl groups and their derivatives identifies a tertiary structure that changes upon light-activationJ Klein-Seetharaman, J Hwa, K Cai, et al.
Proceedings of the National Academy of Sciences of the United States of America|February 7, 1998
Structure and function in rhodopsin: rhodopsin mutants with a neutral amino acid at E134 have a partially activated conformation in the dark stateJ M Kim, C Altenbach, R L Thurmond, et al.
Biochemistry|September 24, 1996
Structural features and light-dependent changes in the cytoplasmic interhelical E-F loop region of rhodopsin: a site-directed spin-labeling studyC Altenbach, K Yang, D L Farrens, et al.
Biochemistry|November 12, 1996
Structure and function in rhodopsin. Cysteines 65 and 316 are in proximity in a rhodopsin mutant as indicated by disulfide formation and interactions between attached spin labelsK Yang, D L Farrens, C Altenbach, et al.
Biochemistry|July 1, 1999
Single-cysteine substitution mutants at amino acid positions 306-321 in rhodopsin, the sequence between the cytoplasmic end of helix VII and the palmitoylation sites: sulfhydryl reactivity and transducin activation reveal a tertiary structureK Cai, J Klein-Seetharaman, D Farrens, et al.
Pageof 4

Showing results (21-30 of 37) with videos related to

Sort By:
Pageof 4
Biochemistry|December 19, 2001
Structure and function in rhodopsin: mapping light-dependent changes in distance between residue 316 in helix 8 and residues in the sequence 60-75, covering the cytoplasmic end of helices TM1 and TM2 and their connection loop CL1C Altenbach, J Klein-Seetharaman, K Cai, et al.
Science (New York, N.Y.)|November 1, 1996
Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsinD L Farrens, C Altenbach, K Yang, et al.
Biochemistry|September 14, 2000
Binding of spin-labeled galactosides to the lactose permease of Escherichia coliM Zhao, T Kálai, K Hideg, et al.
Biochemistry|August 11, 1999
Conformation of the diphtheria toxin T domain in membranes: a site-directed spin-labeling study of the TH8 helix and TL5 loopK J Oh, H Zhan, C Cui, et al.
Biochemistry|October 17, 2001
Probing the dark state tertiary structure in the cytoplasmic domain of rhodopsin: proximities between amino acids deduced from spontaneous disulfide bond formation between Cys316 and engineered cysteines in cytoplasmic loop 1J Klein-Seetharaman, J Hwa, K Cai, et al.
Biochemistry|July 1, 1999
Single-cysteine substitution mutants at amino acid positions 55-75, the sequence connecting the cytoplasmic ends of helices I and II in rhodopsin: reactivity of the sulfhydryl groups and their derivatives identifies a tertiary structure that changes upon light-activationJ Klein-Seetharaman, J Hwa, K Cai, et al.
Proceedings of the National Academy of Sciences of the United States of America|February 7, 1998
Structure and function in rhodopsin: rhodopsin mutants with a neutral amino acid at E134 have a partially activated conformation in the dark stateJ M Kim, C Altenbach, R L Thurmond, et al.
Biochemistry|September 24, 1996
Structural features and light-dependent changes in the cytoplasmic interhelical E-F loop region of rhodopsin: a site-directed spin-labeling studyC Altenbach, K Yang, D L Farrens, et al.
Biochemistry|November 12, 1996
Structure and function in rhodopsin. Cysteines 65 and 316 are in proximity in a rhodopsin mutant as indicated by disulfide formation and interactions between attached spin labelsK Yang, D L Farrens, C Altenbach, et al.
Biochemistry|July 1, 1999
Single-cysteine substitution mutants at amino acid positions 306-321 in rhodopsin, the sequence between the cytoplasmic end of helix VII and the palmitoylation sites: sulfhydryl reactivity and transducin activation reveal a tertiary structureK Cai, J Klein-Seetharaman, D Farrens, et al.
Pageof 4