NMR relaxation unravels interdomain crosstalk of the two domain prolyl isomerase and chaperone SlyD

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1814, Issue 7, 2011, Pages 873-881

  Kovermann, Michael ^a   Zierold, Robert ^a,c   Haupt, Caroline ^a   Löw, Christian ^b   Balbach, Jochen ^a  

^a MARTIN LUTHER UNIVERSITY HALLE WITTENBERG   (Germany)

^b KAROLINSKA INSTITUTE   (Sweden)

^c UNIVERSITY OF HAMBURG   (Germany)

Author keywords

Diffusion; FKBP; Molecular chaperone; NMR dynamics; Prolyl isomerase; Protein folding

Indexed keywords

AMIDE; CHAPERONE; ISOMERASE; PROLINE DERIVATIVE; PROLYL ISOMERASE; PROTON; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; DIFFUSION COEFFICIENT; DYNAMICS; ENZYME SUBSTRATE; ESCHERICHIA COLI; ISOMERIZATION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; SPECIES; TEMPERATURE; THERMUS THERMOPHILUS;

ALGORITHMS; BACTERIAL PROTEINS; BINDING SITES; CATALYTIC DOMAIN; ESCHERICHIA COLI PROTEINS; HUMANS; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR CHAPERONES; PEPTIDE FRAGMENTS; PEPTIDYLPROLYL ISOMERASE; PROTEIN STRUCTURE, TERTIARY; TAT GENE PRODUCTS, HUMAN IMMUNODEFICIENCY VIRUS; TEMPERATURE; THERMUS THERMOPHILUS;

ESCHERICHIA COLI; THERMUS THERMOPHILUS;

EID: 79957605654     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2011.03.016     Document Type: Article

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