NMR solution structure of the precursor for carnobacteriocin B2, an antimicrobial peptide from Carnobacterium piscicola. Implications of the alpha-helical leader section for export and inhibition of type IIa bacteriocin activity

2004 ◽  
Vol 271 (9) ◽  
pp. 1748-1756 ◽  
Author(s):  
Tara Sprules ◽  
Karen E. Kawulka ◽  
Alan C. Gibbs ◽  
David S. Wishart ◽  
John C. Vederas
Keyword(s):  
Antimicrobial Peptide ◽  
Solution Structure ◽  
Bacteriocin Activity ◽  
Nmr Solution Structure ◽  
Carnobacterium Piscicola

scholarly journals NMR Solution Structure and Condition-Dependent Oligomerization of the Antimicrobial Peptide Human Defensin 5

Biochemistry ◽  
2012 ◽  
Vol 51 (48) ◽  
pp. 9624-9637 ◽  
Author(s):  
Andrew J. Wommack ◽  
Scott A. Robson ◽  
Yoshitha A. Wanniarachchi ◽  
Andrea Wan ◽  
Christopher J. Turner ◽  
...  
Keyword(s):  
Antimicrobial Peptide ◽  
Solution Structure ◽  
Nmr Solution Structure ◽  
Human Defensin 5

Revisiting the NMR solution structure of the Cel48S type-I dockerin module from Clostridium thermocellum reveals a cohesin-primed conformation

2014 ◽  
Vol 188 (2) ◽  
pp. 188-193 ◽  
Author(s):  
Chao Chen ◽  
Zhenling Cui ◽  
Yan Xiao ◽  
Qiu Cui ◽  
Steven P. Smith ◽  
...  
Keyword(s):  
Clostridium Thermocellum ◽  
Solution Structure ◽  
Type I ◽  
Nmr Solution Structure

NMR solution structure of the inserted domain of human leukocyte function associated antigen-1

2000 ◽  
Vol 295 (5) ◽  
pp. 1251-1264 ◽  
Author(s):  
Glen B. Legge ◽  
Richard W. Kriwacki ◽  
John Chung ◽  
Ulrich Hommel ◽  
Paul Ramage ◽  
...  
Keyword(s):  
Solution Structure ◽  
Human Leukocyte ◽  
Nmr Solution Structure ◽  
Leukocyte Function

The NMR solution structure of the non-classical homeodomain from the rat liver LFB1/HNF1 transcription factor 1 1Edited by P. E. Wright

1997 ◽  
Vol 267 (3) ◽  
pp. 673-683 ◽  
Author(s):  
Oliver Schott ◽  
Martin Billeter ◽  
Barbara Leiting ◽  
Gerhard Wider ◽  
Kurt Wüthrich
Keyword(s):  
Transcription Factor ◽  
Rat Liver ◽  
Solution Structure ◽  
Nmr Solution Structure ◽  
Transcription Factor 1

scholarly journals Engineering Increased Stability in the Antimicrobial Peptide Pediocin PA-1

2000 ◽  
Vol 66 (11) ◽  
pp. 4798-4802 ◽  
Author(s):  
Line Johnsen ◽  
Gunnar Fimland ◽  
Vincent Eijsink ◽  
Jon Nissen-Meyer
Keyword(s):  
Antimicrobial Peptide ◽  
Molecular Mass ◽  
Room Temperature ◽  
Bacteriocin Activity ◽  
Food Preservative ◽  
Food Grade ◽  
First Order ◽  
Methionine Residue ◽  
First Order Kinetics

ABSTRACT Pediocin PA-1 is a food grade antimicrobial peptide that has been used as a food preservative. Upon storage at 4°C or room temperature, pediocin PA-1 looses activity, and there is a concomitant 16-Da increase in the molecular mass. It is shown that the loss of activity follows first-order kinetics and that the instability can be prevented by replacing the single methionine residue (Met31) in pediocin PA-1. Replacing Met by Ala, Ile, or Leu protected the peptide from oxidation and had only minor effects on bacteriocin activity (for most indicator strains 100% activity was maintained). Replacement of Met by Asp was highly deleterious for bacteriocin activity.

Solution structure of microcin J25, the single macrocyclic antimicrobial peptide from Escherichia coli

2001 ◽  
Vol 268 (7) ◽  
pp. 2124-2133 ◽  
Author(s):  
Alain Blond ◽  
Michel Cheminant ◽  
Isabelle Ségalas-Milazzo ◽  
Jean Péduzzi ◽  
Michel Barthélémy ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Antimicrobial Peptide ◽  
Solution Structure ◽  
Microcin J25
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