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K Grüner

Publications and source records attributed to K Grüner.

4 recordsLinked to original sources
PubMed2002

Electron-induced neutron knockout from 4He.

The differential cross section for electron-induced neutron knockout in the reaction 4He(e,e(')n)(3)He has been measured for the first time with a statistical accuracy of 11%. The experiment was performed in quasielastic kinematics at a momentum transfer of 300 MeV/c and in the missing-momentum range of 25-70 MeV/c. The comparison of the data with theoretical calculations shows an impressive increase of the cross section resulting from final state interaction effects. Specifically, the p-n charge-exchange process dominates the cross section in this kinematical regime.

Journal Article↗
PubMed1999

The relationship between anxious rearing behaviours and anxiety disorders symptomatology in normal children.

The present study examined the relationship between perceived parental rearing practices, in particular anxious rearing behaviours, and anxiety symptoms. One-hundred and seventeen school children aged between 9 and 12 years completed the EMBU for children, a questionnaire that measures perceptions of parental rearing behaviours, and the Children's Anxiety Scale, an index of DSM-defined anxiety disorders symptoms. Results showed that there were significant and positive associations between Parental Rejection, Anxious Rearing, and Parental Control, on the one hand, and anxiety symptoms, on the other hand Emotional Warmth was not related to anxiety symptoms.

Anxiety↗
PubMed1982

Amino acid sequence of the small cyanogen bromide peptide of thermitase, a thermostable serine proteinase from Thermoactinomyces vulgaris. Relation to the subtilisins.

The following amino acid sequence of the small cyanogen bromide peptide (mol. wt. 5399) of thermitase from Thermoactinomyces vulgaris has been determined: Ala-Thr-Pro-His-Val-Ala-Gly-Val-Ala-Gly-Leu-Leu-Ala-Ser-Gln-Gly-Arg-Ser-Ala-Ser -Asn-Ile-Arg-Ala-Ala-Ile-Glu-Asn-Thr-Ala-Asp-Lys-Ile-Ser-Gly-Thr-Gly-Thr-Tyr-Trp-Ala-Lys-Gly-Arg-Val-Asn-Ala-Tyr-Lys-Ala-Val-Gln-Tyr. The results obtained support the classification of the enzyme as a serine proteinase of the subtilisin type as proposed in a previous paper (1). This partial sequence extending from the serine residue involved in the active site to the C-terminal amino acid of the enzyme shows a 40% homology with the corresponding part of the subtilisin BPN' or subtilisin Carlsberg molecule but a 56% homology as regards conservative amino acid replacements. The secondary structure of this polypeptide fragment, predicted from the data obtained by the method of Chou & Fasman (2) agrees fairly well, within the limit or error of the method, with the structure of the corresponding part of the subtilisin BPN' molecule. Therefore, as expected, no dramatic changes in the spatial structure appear to account for the higher thermostability of thermitase, at least in this area of the polypeptide chain.

Amino Acid Sequence↗