Sequence-specific (1)H, (13)C and (15)N resonance assignments and secondary structure of a truncated protease from Simian Foamy Virus

Maximilian J Hartl; Birgitta M Wöhrl; Kristian Schweimer

doi:10.1007/s12104-007-9048-6

Sequence-specific (1)H, (13)C and (15)N resonance assignments and secondary structure of a truncated protease from Simian Foamy Virus

Biomol NMR Assign. 2007 Dec;1(2):175-7. doi: 10.1007/s12104-007-9048-6. Epub 2007 Sep 18.

Authors

Maximilian J Hartl¹, Birgitta M Wöhrl, Kristian Schweimer

Affiliation

¹ Lehrstuhl Biopolymere, Universität Bayreuth, Germany.

PMID: 19636858
DOI: 10.1007/s12104-007-9048-6

Abstract

The backbone and side chain assignments of the retroviral aspartate protease from Simian Foamy Virus from macaques (SFVmac) have been determined by triple resonance NMR techniques.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Carbon Isotopes / chemistry
Magnetic Resonance Spectroscopy / methods*
Nitrogen Isotopes / chemistry
Peptide Hydrolases / chemistry*
Peptide Hydrolases / ultrastructure*
Protein Structure, Secondary
Protein Structure, Tertiary
Protons
Simian foamy virus / enzymology*

Substances

Carbon Isotopes
Nitrogen Isotopes
Protons
Peptide Hydrolases