Rayleigh scattering of Mössbauer radiation on met-myoglobin

G. U. Nienhaus; F. Parak

doi:10.1007/BF02399508

Rayleigh scattering of Mössbauer radiation on met-myoglobin

G. U. Nienhaus
, F. Parak

University of Münster

Research output: Contribution to journal › Article › peer-review

12 Scopus citations

Abstract

Dynamics of myoglobin were studied by means of the RSMR-method. A large multiwire proportional counter was employed to measure simultaneously the scattered intensity at different angles in an angular range from 9.0° to 19°. The evaluations show that in wet myoglobin molecular segments move collectively with <x²>=0.27 A². Freeze dried myoglobin shows normal solid state vibrations with <x²>=0.06 A².

Original language	English
Pages (from-to)	1451-1454
Number of pages	4
Journal	Hyperfine Interactions
Volume	29
Issue number	1-4
DOIs	https://doi.org/10.1007/BF02399508
State	Published - Feb 1986
Externally published	Yes

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@article{ac1e6d59452a45a8a34bdbff2a1b9f2d,

title = "Rayleigh scattering of M{\"o}ssbauer radiation on met-myoglobin",

abstract = "Dynamics of myoglobin were studied by means of the RSMR-method. A large multiwire proportional counter was employed to measure simultaneously the scattered intensity at different angles in an angular range from 9.0° to 19°. The evaluations show that in wet myoglobin molecular segments move collectively with 2>=0.27 A2. Freeze dried myoglobin shows normal solid state vibrations with 2>=0.06 A2.",

author = "Nienhaus, \{G. U.\} and F. Parak",

year = "1986",

month = feb,

doi = "10.1007/BF02399508",

language = "English",

volume = "29",

pages = "1451--1454",

journal = "Hyperfine Interactions",

issn = "0304-3843",

publisher = "Springer Nature",

number = "1-4",

}

TY - JOUR

T1 - Rayleigh scattering of Mössbauer radiation on met-myoglobin

AU - Nienhaus, G. U.

AU - Parak, F.

PY - 1986/2

Y1 - 1986/2

N2 - Dynamics of myoglobin were studied by means of the RSMR-method. A large multiwire proportional counter was employed to measure simultaneously the scattered intensity at different angles in an angular range from 9.0° to 19°. The evaluations show that in wet myoglobin molecular segments move collectively with 2>=0.27 A2. Freeze dried myoglobin shows normal solid state vibrations with 2>=0.06 A2.

AB - Dynamics of myoglobin were studied by means of the RSMR-method. A large multiwire proportional counter was employed to measure simultaneously the scattered intensity at different angles in an angular range from 9.0° to 19°. The evaluations show that in wet myoglobin molecular segments move collectively with 2>=0.27 A2. Freeze dried myoglobin shows normal solid state vibrations with 2>=0.06 A2.

UR - https://www.scopus.com/pages/publications/0000565311

U2 - 10.1007/BF02399508

DO - 10.1007/BF02399508

M3 - Article

AN - SCOPUS:0000565311

SN - 0304-3843

VL - 29

SP - 1451

EP - 1454

JO - Hyperfine Interactions

JF - Hyperfine Interactions

IS - 1-4

ER -

Rayleigh scattering of Mössbauer radiation on met-myoglobin

Abstract

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