Conformational studies of an undecapeptide reproducing the consensus sequence around the cleavage site of the RXVRG endoprotease from Xenopus laevis skin

Biopolymers

Volumn 34, Issue 10, 1994, Pages 1419-1431

  Baron, Daniel ^a   Leseney, Anne‐Marie ^b   Chalaoux, Francois‐Regis ^a   Riand, Jacques ^a  

^a UNIVERSITÉ DES SCIENCES ET TECHNOLOGIES DE LILLE   (France)

^b SORBONNE UNIVERSITÉ   (France)

Author keywords

[No Author keywords available]

Indexed keywords

DIMETHYL SULFOXIDE; PROTEINASE;

AMINO ACID SEQUENCE; ARTICLE; ENZYME ACTIVITY; ENZYME CONFORMATION; HYDROGEN BOND; NONHUMAN; NUCLEAR OVERHAUSER EFFECT; PROTEIN DEGRADATION; SKIN; STRUCTURE ANALYSIS; XENOPUS LAEVIS;

AMINO ACID SEQUENCE; ANIMAL; BINDING SITES; ENDOPEPTIDASES; METALLOENDOPEPTIDASES; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; SKIN; XENOPUS LAEVIS;

XENOPUS LAEVIS;

ASSOCIATION REACTIONS; CATALYST ACTIVITY; CORRELATION METHODS; ENZYMES; HORMONES; MOLECULAR STRUCTURE; NUCLEAR MAGNETIC RESONANCE; SKIN; SOLUTIONS;

CLEAVAGE SITE; CONFORMATIONS; CONSENSUS SEQUENCE; CORRELATED SPECTROSCOPY; ENDOPROTEASE; NUCLEAR OVERHAUSER EFFECT (NOE) SPECTROSCOPY; XENOPUS LAEVIS;

POLYPEPTIDES;

EID: 0028026133     PISSN: 00063525     EISSN: 10970282     Source Type: Journal    
DOI: 10.1002/bip.360341013     Document Type: Article

References (46)

1. Synthetic peptide substrates as models to study a pro-ocytocin/neurophysin converting enzyme
2. A 500-MHz proton nuclear magnetic resonance study of .mu. opioid peptides in a simulated receptor environment
3. Method for evaluating the reliability of distances and rotational correlation times deduced from 2D1H NMR NOESY experiments
4. High-speed Computers as Supplement to Graphical Methods. I. Functional Behavior of the Error Square Sum.