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Volumn 23, Issue 12, 2010, Pages 911-918
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Sequence and structural analysis of two designed proteins with 88 identity adopting different folds
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Author keywords
conformational switch; nucleation site; pentapeptide search; protein folding; surrounding hydrophobicity
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Indexed keywords
AMINO ACID RESIDUES;
CONFORMATIONAL SWITCHES;
CONFORMATIONAL SWITCHING;
INTER-RESIDUE CONTACT;
INTER-RESIDUE INTERACTIONS;
NATURAL PHENOMENA;
NUCLEATION SITE;
PENTAPEPTIDE SEARCH;
PROTEIN ENGINEERING;
SECONDARY STRUCTURE PREDICTION;
SEQUENCE IDENTITY;
STRAND CONFORMATION;
SURROUNDING HYDROPHOBICITY;
THEORETICAL MODELS;
THREE-DIMENSIONAL STRUCTURE;
AMINO ACIDS;
BIOCHEMICAL ENGINEERING;
GENETIC ENGINEERING;
HYDROPHOBICITY;
NUCLEATION;
STRUCTURAL ANALYSIS;
TOPOLOGY;
PROTEIN FOLDING;
AMINO ACID SEQUENCE;
ARTICLE;
CARBOXY TERMINAL SEQUENCE;
HYDROPHOBICITY;
PRIORITY JOURNAL;
PROTEIN CONFORMATION;
PROTEIN FOLDING;
PROTEIN FUNCTION;
PROTEIN INTERACTION;
PROTEIN SECONDARY STRUCTURE;
PROTEIN STRUCTURE;
SEQUENCE ANALYSIS;
STRUCTURE ANALYSIS;
AMINO ACID SEQUENCE;
HYDROPHOBIC AND HYDROPHILIC INTERACTIONS;
MOLECULAR SEQUENCE ANNOTATION;
MOLECULAR SEQUENCE DATA;
PROTEIN ENGINEERING;
PROTEIN FOLDING;
PROTEIN STABILITY;
PROTEIN STRUCTURE, TERTIARY;
PROTEINS;
SEQUENCE ALIGNMENT;
SEQUENCE ANALYSIS, PROTEIN;
SEQUENCE HOMOLOGY, AMINO ACID;
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EID: 78649274872
PISSN: 17410126
EISSN: 17410134
Source Type: Journal
DOI: 10.1093/protein/gzq070 Document Type: Article |
Times cited : (17)
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References (30)
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