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Volumn 41, Issue 1, 2002, Pages 117-119
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De novo protein surface design: Use of cation-π interactions to enhance binding between an α-helical peptide and a cationic molecule in 50% aqueous solution
a
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Author keywords
Helical structures; Host guest systems; Molecular recognition; NMR spectroscopy; Noncovalent interactions
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Indexed keywords
HYDROGEN BONDS;
NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;
POSITIVE IONS;
SOLUTIONS;
SURFACE DESIGN;
PROTEINS;
ASPARTIC ACID;
CATION;
PEPTIDE;
TRYPTOPHAN;
ALPHA HELIX;
AQUEOUS SOLUTION;
ARTICLE;
BINDING AFFINITY;
CHEMISTRY;
CIRCULAR DICHROISM;
HYDROGEN BOND;
MOLECULAR INTERACTION;
MOLECULAR RECOGNITION;
NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;
PROTEIN BINDING;
PROTEIN CONFORMATION;
PROTEIN ENGINEERING;
PROTEIN SECONDARY STRUCTURE;
PROTEIN SYNTHESIS;
SOLUTION AND SOLUBILITY;
SYNTHESIS;
REVIEW;
ASPARTIC ACID;
CATIONS;
HYDROGEN BONDING;
PEPTIDES;
PROTEIN BINDING;
PROTEIN ENGINEERING;
PROTEIN STRUCTURE, SECONDARY;
SOLUTIONS;
SUPPORT, NON-U.S. GOV'T;
SUPPORT, U.S. GOV'T, P.H.S.;
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EID: 0037016255
PISSN: 14337851
EISSN: None
Source Type: Journal
DOI: 10.1002/1521-3773(20020104)41:1<117::AID-ANIE117>3.0.CO;2-J Document Type: Article |
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Times cited : (51)
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References (18)
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