Conformational substates and motions in myoglobin. External influences on structure and dynamics

M. K. Hong, D. Braunstein, B. R. Cowen, H. Frauenfelder, I. E T Iben, J. R. Mourant, P. Ormos, R. Scholl, A. Schulte, P. J. Steinbach, A. H. Xie, R. D. Young

Research output: Contribution to journalArticle

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Abstract

Myoglobin, a simple dioxygen-storage protein, is a good laboratory for the investigation of the connection between protein structure, dynamics, and function. Fourier-transform infrared spectroscopy on carbon-monoxymyoglobin (MbCO) shows three major CO bands. These bands are excellent probes for the investigation of the structure-function relationship. They have different CO binding kinetics and their CO dipoles form different angles with respect to the heme normal, implying that MbCO exists in three major conformational substates, A0, A1, and A3. The entropies and enthalpies of these substates depend on temperature above ~ 180 K and are influenced by pH, solven, and pressure. These results suggest that even a protein as simple as Mb can assume a small number of clearly differerent structures that perform the same function, but with different rates. Moreover, protein structure and dynamics depend strongly on the interaction of the protein with its environment.

Original languageEnglish
Pages (from-to)429-436
Number of pages8
JournalBiophysical Journal
Volume58
Issue number2
Publication statusPublished - 1990

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Myoglobin
Carbon Monoxide
Proteins
Entropy
Fourier Transform Infrared Spectroscopy
Heme
Carbon
Oxygen
Pressure
Temperature

ASJC Scopus subject areas

  • Biophysics

Cite this

Hong, M. K., Braunstein, D., Cowen, B. R., Frauenfelder, H., Iben, I. E. T., Mourant, J. R., ... Young, R. D. (1990). Conformational substates and motions in myoglobin. External influences on structure and dynamics. Biophysical Journal, 58(2), 429-436.

Conformational substates and motions in myoglobin. External influences on structure and dynamics. / Hong, M. K.; Braunstein, D.; Cowen, B. R.; Frauenfelder, H.; Iben, I. E T; Mourant, J. R.; Ormos, P.; Scholl, R.; Schulte, A.; Steinbach, P. J.; Xie, A. H.; Young, R. D.

In: Biophysical Journal, Vol. 58, No. 2, 1990, p. 429-436.

Research output: Contribution to journalArticle

Hong, MK, Braunstein, D, Cowen, BR, Frauenfelder, H, Iben, IET, Mourant, JR, Ormos, P, Scholl, R, Schulte, A, Steinbach, PJ, Xie, AH & Young, RD 1990, 'Conformational substates and motions in myoglobin. External influences on structure and dynamics', Biophysical Journal, vol. 58, no. 2, pp. 429-436.
Hong MK, Braunstein D, Cowen BR, Frauenfelder H, Iben IET, Mourant JR et al. Conformational substates and motions in myoglobin. External influences on structure and dynamics. Biophysical Journal. 1990;58(2):429-436.
Hong, M. K. ; Braunstein, D. ; Cowen, B. R. ; Frauenfelder, H. ; Iben, I. E T ; Mourant, J. R. ; Ormos, P. ; Scholl, R. ; Schulte, A. ; Steinbach, P. J. ; Xie, A. H. ; Young, R. D. / Conformational substates and motions in myoglobin. External influences on structure and dynamics. In: Biophysical Journal. 1990 ; Vol. 58, No. 2. pp. 429-436.
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