H G Khorana

发表

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.

J. Klein-Seetharaman, H. Khorana, C. Altenbach, 2001, Biochemistry.

Structural studies on transmembrane proteins. 2. Spin labeling of bacteriorhodopsin mutants at unique cysteines.

H. Khorana, C. Altenbach, W. Hubbell, 1989, Biochemistry.

Structure of the interhelical loops and carboxyl terminus of bacteriorhodopsin by X-ray diffraction using site-directed heavy-atom labeling.

H. Khorana, M. P. Heyn, R. Mollaaghababa, 1998, Biochemistry.

Mapping of contact sites in complex formation between light-activated rhodopsin and transducin by covalent crosslinking: Use of a chemically preactivated reagent

H. Khorana, K Cai, H G Khorana, 2001, Proceedings of the National Academy of Sciences of the United States of America.

Denaturation and renaturation of bacteriorhodopsin in detergents and lipid-detergent mixtures.

H. Khorana, E. London, H G Khorana, 1982, The Journal of biological chemistry.

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.

J. Klein-Seetharaman, H. Khorana, C. Altenbach, 2001, Biochemistry.

Transmembrane protein structure: spin labeling of bacteriorhodopsin mutants.

H. Khorana, C. Altenbach, W. Hubbell, 1990, Science.

Structure-function studies on bacteriorhodopsin. IX. Substitutions of tryptophan residues affect protein-retinal interactions in bacteriorhodopsin.

H. Khorana, T. Marti, T. Mogi, 1989, The Journal of biological chemistry.

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.

C Altenbach, K Cai, H G Khorana, 1999, Biochemistry.

Studies on polynucleotides. CXVI. A further study of the T4 ligase-catalyzed joining of DNA at base-paired ends.

H. Khorana, H G Khorana, V Sogaramella, 1972, Journal of molecular biology.

Regeneration of native bacteriorhodopsin structure from fragments.

H. Khorana, H G Khorana, K. S. Huang, 1984, The Journal of biological chemistry.

Structure and function in rhodopsin: Mass spectrometric identification of the abnormal intradiscal disulfide bond in misfolded retinitis pigmentosa mutants

J. Klein-Seetharaman, H. Khorana, J Klein-Seetharaman, 2001, Proceedings of the National Academy of Sciences of the United States of America.

Mapping of the amino acids in membrane-embedded helices that interact with the retinal chromophore in bovine rhodopsin.

H. Khorana, H G Khorana, T A Nakayama, 1991, The Journal of biological chemistry.

Vibrational spectroscopy of bacteriorhodopsin mutants: evidence for the interaction of proline-186 with the retinylidene chromophore.

H. Khorana, T. Marti, T. Mogi, 1990, Biochemistry.

Formation of the meta II photointermediate is accompanied by conformational changes in the cytoplasmic surface of rhodopsin.

H. Khorana, W. Hubbell, H G Khorana, 1993, Biochemistry.

Replacement of aspartic acid-96 by asparagine in bacteriorhodopsin slows both the decay of the M intermediate and the associated proton movement.

H. Khorana, M. Holz, V. Skulachev, 1989, Proceedings of the National Academy of Sciences of the United States of America.

Structure and function in rhodopsin: kinetic studies of retinal binding to purified opsin mutants in defined phospholipid-detergent mixtures serve as probes of the retinal binding pocket.

H. Khorana, P. Reeves, H G Khorana, 1999, Proceedings of the National Academy of Sciences of the United States of America.

Orientation of retinal in bovine rhodopsin determined by cross-linking using a photoactivatable analog of 11-cis-retinal.

H. Khorana, H G Khorana, T A Nakayama, 1990, The Journal of biological chemistry.

Optimal strategies for the chemical and enzymatic synthesis of bihelical deoxyribonucleic acids.

H G Khorana, J H van de Sande, M H Caruthers, 1975, Journal of the American Chemical Society.

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.

J. Klein-Seetharaman, H. Khorana, C. Altenbach, 2001, Biochemistry.

A further study of the T4 ligase-catalyzed joining of DNA at base-paired ends. 1972.

V Sgaramella, H G Khorana, 1992, Biotechnology.

Site of attachment of retinal in bacteriorhodopsin.

R Radhakrishnan, H. Khorana, H. Bayley, 1981, Proceedings of the National Academy of Sciences of the United States of America.

Rhodopsin, the Visual Pigment, and Bacteriorhodopsin a

H G Khorana, 1986, Annals of the New York Academy of Sciences.

Studies on polynucleotides, XLIX. Stimulation of the binding of aminoacyl-sRNA's to ribosomes by ribotrinucleotides and a survey of codon assignments for 20 amino acids.

H. Khorana, D. Söll, E. Ohtsuka, 1965, Proceedings of the National Academy of Sciences of the United States of America.

Refolding of an integral membrane protein. Denaturation, renaturation, and reconstitution of intact bacteriorhodopsin and two proteolytic fragments.

H. Khorana, H. Bayley, E. London, 1981, The Journal of biological chemistry.

Structure and function in rhodopsin: topology of the C-terminal polypeptide chain in relation to the cytoplasmic loops.

H. Khorana, W. Hubbell, R. Langen, 1997, Proceedings of the National Academy of Sciences of the United States of America.

Requirement of Rigid-Body Motion of Transmembrane Helices for Light Activation of Rhodopsin

H. Khorana, C. Altenbach, W. Hubbell, 1996, Science.

Total synthesis of a tyrosine suppressor transfer RNA gene. XVI. Enzymatic joinings to form the total 207-base pair-long DNA.

R. Contreras, H. Khorana, E. Brown, 1979, The Journal of biological chemistry.

Surface charge of bacteriorhodopsin detected with covalently bound pH indicators at selected extracellular and cytoplasmic sites.

H. Khorana, P. Scherrer, M. P. Heyn, 1994, Biochemistry.

Rhodopsin kinase: two mAbs binding near the carboxyl terminus cause time-dependent inactivation.

H. Khorana, P. Reeves, L. Niu, 2000, Proceedings of the National Academy of Sciences of the United States of America.

Substitution of amino acids Asp-85, Asp-212, and Arg-82 in bacteriorhodopsin affects the proton release phase of the pump and the pK of the Schiff base.

H. Khorana, M. Holz, M. P. Heyn, 1990, Proceedings of the National Academy of Sciences of the United States of America.

Structural features and light-dependent changes in the sequence 59-75 connecting helices I and II in rhodopsin: a site-directed spin-labeling study.

J. Klein-Seetharaman, H. Khorana, C. Altenbach, 1999, Biochemistry.

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.

J. Klein-Seetharaman, H. Khorana, C. Altenbach, 2001, Biochemistry.

Detection of a water molecule in the active-site of bacteriorhodopsin: hydrogen bonding changes during the primary photoreaction.

H. Khorana, T. Marti, H G Khorana, 1994, Biochemistry.

Protonation state of Asp (Glu)-85 regulates the purple-to-blue transition in bacteriorhodopsin mutants Arg-82----Ala and Asp-85----Glu: the blue form is inactive in proton translocation.

H. Khorana, T. Marti, H G Khorana, 1990, Proceedings of the National Academy of Sciences of the United States of America.

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.

J. Klein-Seetharaman, H. Khorana, C. Altenbach, 1999, Biochemistry.

Structure and function in rhodopsin. Single cysteine substitution mutants in the cytoplasmic interhelical E-F loop region show position-specific effects in transducin activation.

H G Khorana, W L Hubbell, D L Farrens, 1996, Biochemistry.

Mapping of contact sites in complex formation between transducin and light-activated rhodopsin by covalent crosslinking: Use of a photoactivatable reagent

H. Khorana, K Cai, H G Khorana, 2001, Proceedings of the National Academy of Sciences of the United States of America.

Molecular Biology of Light Transduction by the Mammalian Photoreceptor, Rhodopsin

H. Khorana, H G Khorana, 2000, Journal of biomolecular structure & dynamics.

Studies on polynucleotides. 48. The in vitro synthesis of a co-polypeptide containing two amino acids in alternating sequence dependent upon a DNA-like polymer containing two nucleotides in alternating sequence.

H. Khorana, S. Nishimura, D. S. Jones, 1965, Journal of molecular biology.

Studies on polynucleotides. LXXXVII. The joining of short deoxyribopolynucleotides by DNA-joining enzymes.

H. Khorana, N. Gupta, E. Ohtsuka, 1968, Proceedings of the National Academy of Sciences of the United States of America.

Structure and function in rhodopsin: further elucidation of the role of the intradiscal cysteines, Cys-110, -185, and -187, in rhodopsin folding and function.

J. Klein-Seetharaman, H. Khorana, P. Reeves, 1999, Proceedings of the National Academy of Sciences of the United States of America.

Structure and function in rhodopsin: effects of disulfide cross-links in the cytoplasmic face of rhodopsin on transducin activation and phosphorylation by rhodopsin kinase.

J. Klein-Seetharaman, H. Khorana, W. Hubbell, 1999, Biochemistry.

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.

J. Klein-Seetharaman, H. Khorana, C. Altenbach, 1999, Biochemistry.

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

H. Khorana, C. Altenbach, W. Hubbell, 1996, Biochemistry.