Conformational studies of the α-Helical 28-43 fragment of the B3 domain of the immunoglobulin binding protein G from streptococcus

Biopolymers

Volumn 89, Issue 11, 2008, Pages 1032-1044

  Skwierawska, Agnieszka ^a,b   Rodziewicz Motowidło, Sylwia ^a   Ołdziej, Stanisław ^a,b   Liwo, Adam ^a,b   Scheraga, Harold A ^b  

^a UNIVERSITY OF GDA SK   (Poland)

^b Department of Obstetrics Gynecology   (United States)

Author keywords

B3 domain of protein G; CD; NMR; Peptide structure

Indexed keywords

AMINES; NUCLEAR MAGNETIC RESONANCE; PROTEIN FOLDING; THREE DIMENSIONAL;

A STABLES; B3 DOMAIN OF PROTEIN G; BINDING DOMAINS; BINDING PROTEINS; CD; CONFORMATIONAL STABILITIES; CONFORMATIONAL STUDIES; DIMENSIONAL STRUCTURES; NMR; NMR STUDIES; PEPTIDE STRUCTURE; PROTEIN G; WEAK SIGNALS;

NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

IMMUNOGLOBULIN BINDING FACTOR; PROTEIN G;

ALPHA HELIX; ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; RESIDUE ANALYSIS; STREPTOCOCCUS; TEMPERATURE MEASUREMENT;

BACTERIAL PROTEINS; CIRCULAR DICHROISM; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY;

STREPTOCOCCUS; STREPTOCOCCUS SP. 'GROUP G';

EID: 54949084313     PISSN: 00063525     EISSN: 10970282     Source Type: Journal    
DOI: 10.1002/bip.21056     Document Type: Article

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