SOLUTION STRUCTURE OF BOVINE NEUTROPHIL BETA-DEFENSIN-12 - THE PEPTIDE FOLD OF THE BETA-DEFENSINS IS IDENTICAL TO THAT OF THE CLASSICAL DEFENSINS
Journal Article
Overview
publication date
- October 17, 1995
has subject area
- Animals
- Biochemical Phenomena - Amino Acid Sequence
- Biochemical Phenomena - Protein Folding
- Biochemical Phenomena - Sequence Homology, Amino Acid
- Biochemical Phenomena - Structure-Activity Relationship
- Biophysical Phenomena - Protein Folding
- Blood Proteins
- Cattle
- Cells - Neutrophils
- Cells - Neutrophils
- Female
- Genetic Phenomena - Sequence Homology, Amino Acid
- Hemic and Immune Systems - Neutrophils
- Hydrogen Bonding
- Immune System - Neutrophils
- Immune System - Neutrophils
- Magnetic Resonance Spectroscopy
- Models, Molecular
- Molecular Sequence Data
- Molecular Sequence Data - Amino Acid Sequence
- Myeloid Cells - Neutrophils
- Peptides - Defensins
- Peptides - beta-Defensins
- Pharmacological Phenomena - Structure-Activity Relationship
- Pore Forming Cytotoxic Proteins - Defensins
- Pore Forming Cytotoxic Proteins - beta-Defensins
- Protein Structure, Secondary
- Solutions
has restriction
- closed
Date in CU Experts
- September 9, 2013 9:19 AM
Full Author List
- ZIMMERMANN GR; LEGAULT P; SELSTED ME; PARDI A
author count
- 4
citation count
- 139
published in
- Biochemistry Journal
Other Profiles
International Standard Serial Number (ISSN)
- 0006-2960
Digital Object Identifier (DOI)
Additional Document Info
start page
- 13663
end page
- 13671
volume
- 34
issue
- 41