Factors involved in the stability of isolated β-sheets: Turn sequence, β-sheet twisting, and hydrophobic surface burial

Protein Science

Volumn 13, Issue 4, 2004, Pages 1134-1147

  Santiveri, Clara M ^a,b   Santoro, Jorge ^a   Rico, Manuel ^a   Jiménez, M Angeles ^a  

^a INSTITUTO DE QUÍMICA FÍSICA ROCASOLANO   (Spain)

^b MRC CENTRE FOR PROTEIN ENGINEERING   (United Kingdom)

Author keywords

sheet stability; sheet structure; sheet twist; turn; NMR; Peptide design

Indexed keywords

AMINO ACID; GLYCINE; PROLINE; PROTEIN; TRYPTOPHAN;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; AQUEOUS SOLUTION; ARTICLE; BETA SHEET; CALCULATION; HYDROPHOBICITY; MODEL; NUCLEAR MAGNETIC RESONANCE; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN MOTIF; PROTEIN STABILITY;

AMINO ACID SEQUENCE; HYDROPHOBICITY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDES; PROTEIN STRUCTURE, SECONDARY; THERMODYNAMICS; WATER;

EID: 1842611349     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.03520704     Document Type: Article

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