Minimal transition state charge stabilization of the oxyanion during peptide bond formation by the ribosome

Biochemistry

Volumn 50, Issue 48, 2011, Pages 10491-10498

  Carrasco, Nicolas ^a,b   Hiller, David A ^a   Strobel, Scott A ^a  

^a YALE UNIVERSITY   (United States)

^b QUINNIPIAC UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO GROUP; AMINOACYL; AMINOLYSIS REACTION; BINDING AFFINITIES; CHARGE STABILIZATION; MINIMAL TRANSITION; NEGATIVE CHARGE; NEUTRAL-CHARGE; ORDERED WATER; OXYANIONS; PEPTIDE BOND FORMATION; PROTON SHUTTLE; RIBOSOMAL PROTEINS; SERIES OF TRANSITION; SERINE PROTEASE; TRANSITION STATE; WATER MOLECULE;

AMINATION; AMINO ACIDS; BINDING ENERGY; BIOSYNTHESIS; ENZYME ACTIVITY; FUNCTIONAL GROUPS; HYDROGEN BONDS; MACROMOLECULES; MOLECULAR DYNAMICS; PEPTIDES; STABILIZATION;

POSITIVE IONS;

ANION; FUNCTIONAL GROUP; HYDROGEN; OXYANION; PEPTIDE; RIBOSOME PROTEIN; SERINE PROTEINASE; UNCLASSIFIED DRUG; WATER;

ARTICLE; BINDING AFFINITY; CATALYSIS; CHEMICAL ANALYSIS; CHEMICAL BOND; CONTROLLED STUDY; HYDROGEN BOND; HYPOTHESIS; MOLECULAR MIMICRY; MOLECULE; PEPTIDE BOND; PHASE TRANSITION; PRIORITY JOURNAL; PROTEIN STABILITY; PROTEIN SYNTHESIS; RIBOSOME; STEREOCHEMISTRY;

CATALYSIS; CATALYTIC DOMAIN; HYDROGEN BONDING; PEPTIDE BIOSYNTHESIS; PEPTIDES; PEPTIDYL TRANSFERASES; PROTEIN STABILITY; RIBOSOMAL PROTEINS; RIBOSOMES; STATIC ELECTRICITY;

EID: 82455172072     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi201290s     Document Type: Article

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