Sequential assignment of 1H, 13C and 15N resonances of human carbonic anhydrase I by triple-resonance NMR techniques and extensive amino acid-specific 15N-labeling.
The backbone NMR resonances of human carbonic anhydrase I (HCA I) have been assigned. This protein is one of the largest monomeric proteins assigned so far. The assignment was enabled by a combination of 3D triple-resonance experiments and extensive use of amino acid-specific 15N-labeling. The obtained resonance assignment has been used to evaluate the secondary structure elements present in solution. The solution structure appears to be very similar to the crystal structure, although some differences can be observed. Proton-deuteron exchange experiments have shown that the assignments provide probes that can be used in future studies of HCA I.
Sethson
I
I
Department of Organic Chemistry, Umeå University, Sweden.
Edlund
U
U
Holak
T A
TA
Ross
A
A
Jonsson
B H
BH
D000595:Amino Acid Sequence; D002247:Carbon Isotopes; D002256:Carbonic Anhydrases / Q000737:chemistry* / Q000235:genetics; D003903:Deuterium; D006801:Humans; D006859:Hydrogen / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D015394:Molecular Structure; D009587:Nitrogen Isotopes; D017433:Protein Structure, Secondary; D011522:Protons; D012996:Solutions
D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D011522:Protons; D012996:Solutions; D006859:Hydrogen; D003903:Deuterium; D002256:Carbonic Anhydrases