Enzymes immobilized as crystals. Hydrogen isotope exchange of crystalline lysozyme.

Abstract:

:Immobilization of enzymes by crystallization and subsequent cross-linking provide structures characterized by a regular three-dimensional molecular arrangement and a high packing density. Compared to randomly immobilized enzymes, such structures permit more detailed analysis of the variations in kinetic properties arising from the three-dimensional network or perturbations of the molecular conformations. To obtain information on the effect of crystallization on the dynamic properties of the folded peptide chain in an enzyme molecule, hydrogen exchange rates were measured for both dissolved and crystalline lysozyme over a wide range of pH. Using this method, which reflects molecular oscillations between closely related conformations, no differences were detected between lysozyme in crystalline and dissolved state.

journal_name

Biochimie

journal_title

Biochimie

authors

Tüchsen E,Hvidt A,Ottesen M

doi

10.1016/s0300-9084(80)80101-5

subject

Has Abstract

pub_date

1980-01-01 00:00:00

pages

563-6

issue

8-9

eissn

0300-9084

issn

1638-6183

pii

S0300-9084(80)80101-5

journal_volume

62

pub_type

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