Contiguous O -galactosylation of 4(R)-hydroxy- l -proline residues forms very stable polyproline II helices

Journal of the American Chemical Society

Volumn 132, Issue 14, 2010, Pages 5036-5042

  Owens, Neil W ^a   Stetefeld, Joìrg ^a   LattovaÌ, Erika ^a   Schweizer, Frank ^a  

^a UNIVERSITY OF MANITOBA   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

CIRCULAR DICHROISM; CONFORMATIONAL STABILITIES; D-GALACTOSE; EXTRACELLULAR MATRICES; GALACTOSYLATION; GLYCAN STRUCTURES; GLYCANS; IN-PLANTS; L-PROLINE; LAND PLANTS; MODEL PEPTIDES; MOLECULAR SCAFFOLDS; NATURALLY OCCURRING; O-GLYCOSYLATION; O-LINKED; POLYPROLINE; POLYPROLINE II; POST-TRANSLATIONAL MODIFICATIONS; QUANTITATIVE DATA; REGULAR NETWORKS; SHIELDING EFFECT; STRUCTURAL PROTEINS; STRUCTURAL RIGIDITY; THERMAL MELTING; THERMAL STABILITY; TYPE II;

AMIDES; CARBOHYDRATES; DICHROISM; ESTERIFICATION; GENE TRANSFER; HYDROGEN BONDS; PEPTIDES; PLANT CELL CULTURE; THERMODYNAMIC STABILITY; THERMOGRAVIMETRIC ANALYSIS;

GLYCOSYLATION;

CARBOHYDRATE; GLYCAN; GLYCOPROTEIN; HYDROXYPROLINE; MOLECULAR SCAFFOLD; PEPTIDE; POLYPEPTIDE; PROLINE DERIVATIVE;

ALGA; ARTICLE; CIRCULAR DICHROISM; GALACTOSYLATION; GLYCOSYLATION; HYDROPHILICITY; MOLECULAR MODEL; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDE SYNTHESIS; PLANT CELL; PROTEIN CONFORMATION; PROTEIN PROCESSING; PROTEIN STRUCTURE; THERMOSTABILITY;

GALACTOSE; GLYCOSYLATION; HYDROXYPROLINE; MODELS, MOLECULAR; PEPTIDES; PROTEIN CONFORMATION; STEREOISOMERISM;

EID: 77950800689     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja905724d     Document Type: Article

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