Long-range dynamic effects of point mutations propagate through side chains in the serine protease inhibitor eglin c

Biochemistry

Volumn 43, Issue 39, 2004, Pages 12448-12458

  Clarkson, Michael W ^a   Lee, Andrew L ^a,b  

^a UNIVERSITY OF NORTH CAROLINA SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF NORTH CAROLINA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ELECTROSTATICS; MUTAGENESIS; NUCLEAR MAGNETIC RESONANCE; PERTURBATION TECHNIQUES;

GLOBULAR PROTEINS; NONELECTROSTATIC PERTURBATIONS; SPIN RELAXATION PROPERTIES;

PROTEINS;

ALANINE; EGLIN C; GLOBULAR PROTEIN; SERINE PROTEINASE INHIBITOR; VALINE;

ALLOSTERISM; ARTICLE; DYNAMICS; NITROGEN NUCLEAR MAGNETIC RESONANCE; POINT MUTATION; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTON NUCLEAR MAGNETIC RESONANCE;

ALANINE; ANIMALS; LEECHES; MODELS, CHEMICAL; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; NANOTECHNOLOGY; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PHENYLALANINE; POINT MUTATION; POLYMERASE CHAIN REACTION; PROTEIN CONFORMATION; PROTEIN SUBUNITS; PROTEINS; SERINE PROTEINASE INHIBITORS; SERPINS; THERMODYNAMICS; TRYPTOPHAN; VALINE;

EID: 4744347909     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0494424     Document Type: Article

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