The thermodynamics of association and unfolding of the 205–316 C-terminal fragment of thermolysin-Reference-Cited by-同舟云学术

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The thermodynamics of association and unfolding of the 205–316 C-terminal fragment of thermolysin

Published:1995-09 Issue:1 Volume:1252 Page:95-102
ISSN:0167-4838
Container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology

Author:

Azuaga Ana I,Conejero-Lara Francisco,Rivas Germán,De Filippis Vincenzo,Fontana Angelo,Mateo Pedro L

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Structural Biology

Reference34 articles.

1. Coupling of Local Folding to Site-Specific Binding of Proteins to DNA

2. Folding of Protein Fragments

3. The Conformation of Thermolysin

4. Structure of thermolysin refined at 1.6 Å resolution

5. Domain characteristics of the carboxyl-terminal fragment 206-316 of thermolysin: unfolding thermodynamics

Cited by 7 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. Thermodynamic and structural analysis of homodimeric proteins: Model of β-lactoglobulin;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2012-02

2. Folding of an isolated ribonuclease H core fragment;Protein Science;2008-12-31

3. Detection and Characterization of Partially Unfolded Oligomers of the SH3 Domain of α-Spectrin;Biophysical Journal;2004-04

4. Dimethyl sulfoxide at 2.5% (v/v) alters the structural cooperativity and unfolding mechanism of dimeric bacterial NAD+ synthetase;Protein Science;2004-02-06

5. Differential scanning calorimetry of thermolysin and its 255–316 and 205–316 C-terminal fragments;Reactive and Functional Polymers;1997-09

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