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Volumn 83, Issue 3, 2002, Pages 1268-1280
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Exploring the propensities of helices in PrPC to form β sheet using NMR structures and sequence alignments
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Author keywords
[No Author keywords available]
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Indexed keywords
PRION PROTEIN;
ALPHA HELIX;
AMINO ACID SEQUENCE;
ARTICLE;
BETA SHEET;
CALCULATION;
CONFORMATIONAL TRANSITION;
DEGENERATIVE DISEASE;
NUCLEAR MAGNETIC RESONANCE;
PRION DISEASE;
PROTEIN ANALYSIS;
PROTEIN CONFORMATION;
PROTEIN POLYMERIZATION;
PROTEIN STABILITY;
PROTEIN STRUCTURE;
SCRAPIE;
SEQUENCE ANALYSIS;
ANIMAL;
BIOPHYSICS;
CHEMICAL STRUCTURE;
CHEMISTRY;
CIRCULAR DICHROISM;
DATA BASE;
HYDROGEN BOND;
METABOLISM;
MOLECULAR GENETICS;
NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;
PROTEIN BINDING;
PROTEIN DENATURATION;
PROTEIN FOLDING;
PROTEIN SECONDARY STRUCTURE;
PROTEIN TERTIARY STRUCTURE;
THERMODYNAMICS;
ANAS SP.;
AVES;
GALLUS GALLUS;
MAMMALIA;
AMINO ACID SEQUENCE;
ANIMALS;
BIOPHYSICS;
CIRCULAR DICHROISM;
DATABASES;
HYDROGEN BONDING;
MAGNETIC RESONANCE SPECTROSCOPY;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
PROTEIN BINDING;
PROTEIN CONFORMATION;
PROTEIN DENATURATION;
PROTEIN FOLDING;
PROTEIN STRUCTURE, SECONDARY;
PROTEIN STRUCTURE, TERTIARY;
PRPC PROTEINS;
THERMODYNAMICS;
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EID: 0036708438
PISSN: 00063495
EISSN: None
Source Type: Journal
DOI: 10.1016/S0006-3495(02)73899-X Document Type: Article |
Times cited : (94)
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References (49)
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