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Volumn 14, Issue 19, 2000, Pages 1736-1745
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Evaluation of the metal binding properties of the histidine-rich antimicrobial peptides histatin 3 and 5 by electrospray ionization mass spectrometry
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Author keywords
[No Author keywords available]
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Indexed keywords
AMINO ACIDS;
BINDING ENERGY;
BINDING SITES;
CIRCULAR DICHROISM SPECTROSCOPY;
DICHROISM;
ELECTRODEPOSITION;
ELECTROSPRAY IONIZATION;
MASS SPECTROMETRY;
METAL IONS;
ANTIMICROBIAL PEPTIDE;
CONFORMATIONAL CHANGE;
ELECTROSPRAY IONIZATION MASS SPECTROMETRY;
HIGH AFFINITY;
HISTATIN;
METAL BINDING PROPERTIES;
METAL ION INTERACTIONS;
METALS IONS;
MULTIPLE BINDING SITES;
ZN 2+;
PEPTIDES;
COPPER COMPLEX;
DIVALENT CATION;
GLYCOPROTEIN;
HISTATIN;
HISTATIN 3;
HISTATIN 5;
HISTIDINE;
METAL;
METAL ION;
NICKEL COMPLEX;
PROTEIN;
SALIVA PROTEIN;
UNCLASSIFIED DRUG;
ZINC COMPLEX;
AMINO ACID SEQUENCE;
ANTIMICROBIAL ACTIVITY;
ARTICLE;
BINDING AFFINITY;
BINDING SITE;
CHEMISTRY;
CIRCULAR DICHROISM;
CONFORMATIONAL TRANSITION;
MASS SPECTROMETRY;
METAL BINDING;
MOLECULAR GENETICS;
PH;
PROTEIN BINDING;
PROTEIN CONFORMATION;
PROTEIN DENATURATION;
PROTEIN SECONDARY STRUCTURE;
PROTEIN STABILITY;
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EID: 0033794888
PISSN: 09514198
EISSN: None
Source Type: Journal
DOI: 10.1002/1097-0231(20001015)14:19<1736::AID-RCM86>3.0.CO;2-2 Document Type: Article |
Times cited : (47)
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References (21)
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