Studies of conformational preferences of derivatives fragments of protein G (1IGD) using temperature dependent potentiometric titration methodology-Reference-Cited by-同舟云学术

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Studies of conformational preferences of derivatives fragments of protein G (1IGD) using temperature dependent potentiometric titration methodology

Published:2014-03 Issue: Volume:70 Page:88-94
ISSN:0021-9614
Container-title:The Journal of Chemical Thermodynamics
language:en
Short-container-title:The Journal of Chemical Thermodynamics

Author:

Makowska Joanna,Uber Dorota,Lubowiecka Dagmara,Chmurzyński Lech

Funder

University of Gdansk

Polish National Science Centre

Publisher

Elsevier BV

Subject

Physical and Theoretical Chemistry,General Materials Science,Atomic and Molecular Physics, and Optics

Reference33 articles.

1. A short linear peptide derived from the N-terminal sequence of ubiquitin folds into a water-stable non-native β-hairpin

2. Dominant forces in protein folding

3. INTERMEDIATES IN THE FOLDING REACTIONS OF SMALL PROTEINS

4. Helix-coil transition of the isolated amino terminus of ribonuclease

5. Nuclear magnetic resonance study of the N-terminal fragment of bovine pancreatic ribonuclease

Cited by 2 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Physicochemical and Structural Studies on Shaping of β-hairpin in Proteins as a First Stage of Amyloid Formation;Current Protein & Peptide Science;2017-10-09

2. A Study of the Influence of Charged Residues on β-Hairpin Formation by Nuclear Magnetic Resonance and Molecular Dynamics;The Protein Journal;2014-10-15

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