Cis/trans heterogeneity of Gln30-Pro31 peptide bond determines whether a 79-residue fragment of staphylococcal nuclease self-associates
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference16 articles.
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2. Searching for folding initiation sites of staphylococcal nuclease: a study of N-terminal short fragments;Dai;Biopolymers,2004
3. Interactions between subdomains in the partially folded state of staphylococcal nuclease;Ye;Biochim. Biophys. Acta,2000
4. Native-like partially folded conformations and folding process revealed in the N-terminal large fragments of staphylococcal nuclease: a study by NMR spectroscopy;Feng;J. Mol. Biol.,2003
5. Self-association reaction of denatured staphylococcal nuclease fragments characterized by heteronuclear NMR;Ye;J. Mol. Biol.,2001
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1. Restricted Backbone Conformational and Motional Flexibilities of Loops Containing Peptidyl−Proline Bonds Dominate the Enzyme Activity of Staphylococcal Nuclease,;Biochemistry;2007-09-22
2. Folding Stability and Cooperativity of the Three Forms of 1–110 Residues Fragment of Staphylococcal Nuclease;Biophysical Journal;2007-03
3. Assignment of paramagnetic 15N-HSQC spectra by heteronuclear exchange spectroscopy;Journal of Biomolecular NMR;2006-11-10
4. Two peptide fragments G55-I72 and K97-A109 from staphylococcal nuclease exhibit different behaviors in conformational preferences for helix formation;Biopolymers;2006-10-15
5. Probing the folding capacity and residual structures in 1–79 residues fragment of staphylococcal nuclease by biophysical and NMR methods;Biochimie;2006-10
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