Excitations in Metmyoglobin crystals at low temperatures

G. P. Singh, H. J. Schink, H. v. Löhneysen, F. Parak, S. Hunklinger

Research output: Contribution to journalArticlepeer-review

73 Scopus citations


Specific heat and dielectric constant of Metmyoglobin crystals at low temperatures are measured and found to be similar to those of amorphous dielectrics. This provides evidence for the existence of two level systems in the protein. Possibility of many conformational substates and the frozen in disorder in the protein is proposed as the origin of these excitations.

Original languageEnglish
Pages (from-to)23-26
Number of pages4
JournalZeitschrift für Physik B Condensed Matter
Issue number1
StatePublished - Mar 1984
Externally publishedYes


Dive into the research topics of 'Excitations in Metmyoglobin crystals at low temperatures'. Together they form a unique fingerprint.

Cite this