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Results: 1-6 |
Results: 6
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 1
Authors: Klein-Seetharaman, J Hwa, J Cai, KW Altenbach, C Hubbell, WL Khorana, HG
Citation: J. Klein-seetharaman et al., 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 1, BIOCHEM, 40(42), 2001, pp. 12472-12478
Probing the dark state tertiary structure in the cytoplasmic domain of rhodopsin: Proximities between amino acids deduced from spontaneous disulfide bond formation between cysteine pairs engineered in cytoplasmic loops 1, 3,and 4
Authors: Cai, KW Klein-Seetharaman, J Altenbach, C Hubbell, WL Khorana, HG
Citation: Kw. Cai et al., Probing the dark state tertiary structure in the cytoplasmic domain of rhodopsin: Proximities between amino acids deduced from spontaneous disulfide bond formation between cysteine pairs engineered in cytoplasmic loops 1, 3,and 4, BIOCHEM, 40(42), 2001, pp. 12479-12485
Structural features of the C-terminal domain of bovine rhodopsin: A site-directed spin-labeling study
Authors: Langen, R Cai, KW Altenbach, C Khorana, HG Hubbell, WL
Citation: R. Langen et al., Structural features of the C-terminal domain of bovine rhodopsin: A site-directed spin-labeling study, BIOCHEM, 38(25), 1999, pp. 7918-7924
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 structure
Authors: Cai, KW Klein-Seetharaman, J Farrens, D Zhang, C Altenbach, C Hubbell, WL Khorana, HG
Citation: Kw. Cai et al., 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 structure, BIOCHEM, 38(25), 1999, pp. 7925-7930
Structural features and light-dependent changes in the sequence 306-322 extending from helix VII to the palmitoylation sites in rhodopsin: A site-directed spin-labeling study
Authors: Altenbach, C Cai, KW Khorana, HG Hubbell, WL
Citation: C. Altenbach et al., Structural features and light-dependent changes in the sequence 306-322 extending from helix VII to the palmitoylation sites in rhodopsin: A site-directed spin-labeling study, BIOCHEM, 38(25), 1999, pp. 7931-7937
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-activation
Authors: Klein-Seetharaman, J Hwa, J Cai, KW Altenbach, C Hubbell, WL Khorana, HG
Citation: J. Klein-seetharaman et al., 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-activation, BIOCHEM, 38(25), 1999, pp. 7938-7944
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