NMR spectroscopy in studies of light-induced structural changes in mammalian rhodopsin: Applicability of solution 19F NMR
Author:
Publisher
Proceedings of the National Academy of Sciences
Subject
Multidisciplinary
Reference41 articles.
1. 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,
2. 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,
3. 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,
4. Structural Features and Light-Dependent Changes in the Sequence 59−75 Connecting Helices I and II in Rhodopsin: A Site-Directed Spin-Labeling Study,
5. Arrangement of rhodopsin transmembrane α-helices
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