Hubbell WL - Search Results

1

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 labels.

Yang K, Farrens DL, Altenbach C, Farahbakhsh ZT, Hubbell WL, Khorana HG. Yang K, et al. Among authors: hubbell wl. Biochemistry. 1996 Nov 12;35(45):14040-6. doi: 10.1021/bi962113u. Biochemistry. 1996. PMID: 8916888

2

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.

Klein-Seetharaman J, Hwa J, Cai K, Altenbach C, Hubbell WL, Khorana HG. Klein-Seetharaman J, et al. Among authors: hubbell wl. Biochemistry. 2001 Oct 23;40(42):12472-8. doi: 10.1021/bi010746p. Biochemistry. 2001. PMID: 11601970

3

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.

Cai K, Klein-Seetharaman J, Altenbach C, Hubbell WL, Khorana HG. Cai K, et al. Among authors: hubbell wl. Biochemistry. 2001 Oct 23;40(42):12479-85. doi: 10.1021/bi010747h. Biochemistry. 2001. PMID: 11601971

4

Structure and function in rhodopsin: mapping light-dependent changes in distance between residue 65 in helix TM1 and residues in the sequence 306-319 at the cytoplasmic end of helix TM7 and in helix H8.

Altenbach C, Cai K, Klein-Seetharaman J, Khorana HG, Hubbell WL. Altenbach C, et al. Among authors: hubbell wl. Biochemistry. 2001 Dec 25;40(51):15483-92. doi: 10.1021/bi011546g. Biochemistry. 2001. PMID: 11747423

5

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 CL1.

Altenbach C, Klein-Seetharaman J, Cai K, Khorana HG, Hubbell WL. Altenbach C, et al. Among authors: hubbell wl. Biochemistry. 2001 Dec 25;40(51):15493-500. doi: 10.1021/bi011545o. Biochemistry. 2001. PMID: 11747424

6

Structural features and light-dependent changes in the cytoplasmic interhelical E-F loop region of rhodopsin: a site-directed spin-labeling study.

Altenbach C, Yang K, Farrens DL, Farahbakhsh ZT, Khorana HG, Hubbell WL. Altenbach C, et al. Among authors: hubbell wl. Biochemistry. 1996 Sep 24;35(38):12470-8. doi: 10.1021/bi960849l. Biochemistry. 1996. PMID: 8823182

7

Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin.

Farrens DL, Altenbach C, Yang K, Hubbell WL, Khorana HG. Farrens DL, et al. Among authors: hubbell wl. Science. 1996 Nov 1;274(5288):768-70. doi: 10.1126/science.274.5288.768. Science. 1996. PMID: 8864113

8

Structure and function in rhodopsin: rhodopsin mutants with a neutral amino acid at E134 have a partially activated conformation in the dark state.

Kim JM, Altenbach C, Thurmond RL, Khorana HG, Hubbell WL. Kim JM, et al. Among authors: hubbell wl. Proc Natl Acad Sci U S A. 1997 Dec 23;94(26):14273-8. doi: 10.1073/pnas.94.26.14273. Proc Natl Acad Sci U S A. 1997. PMID: 9405602 Free PMC article.

9

Structural features of the C-terminal domain of bovine rhodopsin: a site-directed spin-labeling study.

Langen R, Cai K, Altenbach C, Khorana HG, Hubbell WL. Langen R, et al. Among authors: hubbell wl. Biochemistry. 1999 Jun 22;38(25):7918-24. doi: 10.1021/bi990010g. Biochemistry. 1999. PMID: 10387033

10

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.

Cai K, Klein-Seetharaman J, Farrens D, Zhang C, Altenbach C, Hubbell WL, Khorana HG. Cai K, et al. Among authors: hubbell wl. Biochemistry. 1999 Jun 22;38(25):7925-30. doi: 10.1021/bi9900119. Biochemistry. 1999. PMID: 10387034

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