Residual helical and turn structure in the denatured state of staphylococcal nuclease: Analysis of peptide fragments

Folding and Design

Volumn 2, Issue 2, 1997, Pages 93-100

  Wang, Yi ^a   Shortle, David ^a  

^a JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Alpha helices; Beta turns; Denatured proteins; Peptides; Schellman motif

Indexed keywords

MICROCOCCAL NUCLEASE; PEPTIDE FRAGMENT;

AMINO ACID SEQUENCE; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; CIRCULAR DICHROISM; COMPARATIVE STUDY; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN DENATURATION; PROTEIN SECONDARY STRUCTURE;

AMINO ACID SEQUENCE; CIRCULAR DICHROISM; MAGNETIC RESONANCE SPECTROSCOPY; MICROCOCCAL NUCLEASE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PROTEIN DENATURATION; PROTEIN STRUCTURE, SECONDARY;

EID: 0030628174     PISSN: 13590278     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-0278(97)00013-8     Document Type: Article

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