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Volumn 42, Issue 2, 2001, Pages 237-242
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A protein dissection study demonstrates that two specific hydrophobic clusters play a key role in stabilizing the core structure of the molten globule state of human α-lactalbumin
a a a |
Author keywords
lactalbumin; Denatured state; Hydrophobic interactions; Molten globule; Protein folding
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Indexed keywords
ALPHA LACTALBUMIN;
ALPHA HELIX;
CONFERENCE PAPER;
CROSS LINKING;
HYDROPHOBICITY;
PEPTIDE SYNTHESIS;
PRIORITY JOURNAL;
PROTEIN ANALYSIS;
PROTEIN DENATURATION;
PROTEIN FOLDING;
PROTEIN INTERACTION;
PROTEIN STABILITY;
X RAY CRYSTALLOGRAPHY;
AMINO ACID SEQUENCE;
CIRCULAR DICHROISM;
HUMANS;
LACTALBUMIN;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
PEPTIDES;
PROTEIN CONFORMATION;
PROTEIN DENATURATION;
PROTEIN FOLDING;
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EID: 0035254984
PISSN: 08873585
EISSN: None
Source Type: Journal
DOI: 10.1002/1097-0134(20010201)42:2<237::AID-PROT110>3.0.CO;2-B Document Type: Conference Paper |
Times cited : (22)
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References (24)
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