Differential scanning calorimetry of a conformational transition in heavy meromyosin
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference17 articles.
1. The structure of myosin and its role in energy transduction in muscle
2. Phosphorus-31 nuclear magnetic resonance evidence for two conformations of myosin subfragment-1.cntdot.nucleotide complexes
3. Energetics and kinetics of the interconversion of two myosin subfragment-1.cntdot.adenosine 5'-diphosphate complexes as viewed by phosphorus-31 nuclear magnetic resonance
4. Temperature Induced Analog Reaction of Adenylyl Imidodiphosphate to an Intermediate Step of Heavy Meromyosin Adenosine Triphosphatase1
5. Characterization of tHermotropic State Changes in Myosin Subfragment-1 and Heavy Meromyosin by UV Difference Spectroscopy
Cited by 3 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. Simultaneous differential scanning calorimetry, X-ray diffraction and FTIR spectrometry in studies of ovalbumin denaturation;International Journal of Peptide and Protein Research;2009-01-12
2. [9] Calorimetric methods for interpreting protein—Ligand interactions;Methods in Enzymology;1995
3. Protein adsorption on low-temperature isotropic carbon: I. Protein conformational change probed by differential scanning calorimetry;Journal of Biomedical Materials Research;1994-06
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