Primary structure of helix C to helix G of a new retinal protein in H.sp.xz515

Chinese Science Bulletin

Volumn 45, Issue 12, 2000, Pages 1108-1113

  Wang, H ^a   Zhan, S ^a   Sun, Q ^a   Xu, D ^a   Zhao, W ^a   Huang, W ^a   Li, Q ^a  

^a FUDAN UNIVERSITY   (China)

Author keywords

Claret membrane; Halobacteria; PCR; Sequence

Indexed keywords

ARCHAERHODOPSIN; BACTERIAL PROTEIN; BACTERIORHODOPSIN; PROTEIN AR 1; PROTEIN AR 2; PROTON PUMP; RETINA PROTEIN; RETINAL; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; DNA SEQUENCE; HALOBACTERIUM; ISOMERISM; NONHUMAN; NUCLEOTIDE SEQUENCE; POLYMERASE CHAIN REACTION;

BACTERIA (MICROORGANISMS); HALOBACTERIA; HALOBACTERIUM;

EID: 0034479601     PISSN: 10016538     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF02887184     Document Type: Article

References (13)

1. The detection of retinal protein similar to bacteriorhodopsin in four halobacterium species
2. The isolation and purification of archaerhodopsin from Halobacterium sp.xz515
3. Photochemical and proton pumping properties of archaerhodopsin in halobacteria H.sp.xz515
4. The primary structure of helixes A to G of three new bacteriorhodopsin-like retinal proteins
5. Comparative studies on ion pumps of the bacterial rhodopsin family
6. Met-145 is a key residue in the dark-adaptation of bacteriorhodopsin homologs
7. The isolation of the bacteriorhodopsin
8. A simple method for displaying the hydropathic character of a protein
9. Model for the structure of bacteriorhodopsin based on high-resolution electro cryo-microscopy
10. pH dependence of the absorption spectra and photochemical transformations of the archaerhodopsins
11. Relationship of proton uptake on the cytoplasmic surface and the reisomerization of the retinal in the bacteriorhodopsin photocycle: An attempt to understand the complex kinetics of the protons and the N and O intermediates
12. X-ray structure of bacteriorhodopsin at 2.5 A from microcrystal grown in lipidiccubic phases
13. Proton transfer pathways in bacteriorhodopsin at 2.3 angestrom resolution