|
Volumn 890, Issue 1, 2000, Pages 81-94
|
Trapping the monomeric α-helical state during unfolding of coiled-coils by reversed-phase liquid chromatography
|
Author keywords
Peptides; Protein coiled cells; Protein folding; Proteins
|
Indexed keywords
GLUTAMIC ACID;
PEPTIDE;
PROTEIN;
TRIFLUOROETHANOL;
ALPHA HELIX;
ARTICLE;
CIRCULAR DICHROISM;
PRIORITY JOURNAL;
PROTEIN CONFORMATION;
PROTEIN CROSS LINKING;
PROTEIN DENATURATION;
PROTEIN FOLDING;
PROTEIN MODIFICATION;
PROTEIN STABILITY;
REVERSED PHASE LIQUID CHROMATOGRAPHY;
AMINO ACID SEQUENCE;
CHROMATOGRAPHY, LIQUID;
CIRCULAR DICHROISM;
MOLECULAR SEQUENCE DATA;
PEPTIDES;
PROTEIN FOLDING;
PROTEIN STRUCTURE, SECONDARY;
SEQUENCE HOMOLOGY, AMINO ACID;
SPECTROPHOTOMETRY, ULTRAVIOLET;
TEMPERATURE;
|
EID: 0034683139
PISSN: 00219673
EISSN: None
Source Type: Journal
DOI: 10.1016/S0021-9673(00)00472-6 Document Type: Article |
Times cited : (14)
|
References (41)
|