Zobrazeno 1 - 10
of 167
pro vyhledávání: '"T, Kiefhaber"'
Akademický článek
Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
K zobrazení výsledku je třeba se přihlásit.
K zobrazení výsledku je třeba se přihlásit.
Akademický článek
Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
K zobrazení výsledku je třeba se přihlásit.
K zobrazení výsledku je třeba se přihlásit.
Autor:
B. Heinz, B. Schmidt, C. Root, H. Satzger, F. Milota, B. Fierz, T. Kiefhaber, W. Zinth, P. Gilch
Publikováno v:
15th International Conference on Ultrafast Phenomena.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9822257cd907330805f69debf6a2f39c
https://doi.org/10.1364/up.2006.mi9
https://doi.org/10.1364/up.2006.mi9
Publikováno v:
Nature structural biology. 8(5)
Folding of tendamistat, an inhibitor of alpha-amylase, is a fast two-state process accompanied by two minor slow reactions, which were assigned to prolyl isomerization. In a proline-free variant, 5% of the molecules still fold slowly with a rate cons
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::da8fa4cdad0d5aa59ce21726f73486ac
https://pubmed.ncbi.nlm.nih.gov/11323705
https://pubmed.ncbi.nlm.nih.gov/11323705
Autor:
A, Bachmann, T, Kiefhaber
Publikováno v:
Journal of molecular biology. 306(2)
The small all-beta-sheet protein tendamistat folds and unfolds rapidly in apparent two-state reactions. Kinetic measurements of two tendamistat variants under various solvent conditions reveal, however, that folding occurs in at least two sequential
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::1017a09d1d27df57faf2ec01d83395ad
https://pubmed.ncbi.nlm.nih.gov/11237606
https://pubmed.ncbi.nlm.nih.gov/11237606
Publikováno v:
Journal of molecular biology. 268(2)
We investigated the reversible folding and unfolding reactions of the small 74 amino acid residue protein tendamistat. The secondary structure of tendamistat contains only beta-sheets and loop regions and the protein contains two disulfide bonds. Flu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::f8f3719e3cb858e44fb14d3c9aa97241
https://pubmed.ncbi.nlm.nih.gov/9159488
https://pubmed.ncbi.nlm.nih.gov/9159488
Autor:
T, Kiefhaber
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 40
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::08b9c7de884e98b0f7109b58c81eb498
https://pubmed.ncbi.nlm.nih.gov/7633528
https://pubmed.ncbi.nlm.nih.gov/7633528
Autor:
T, Kiefhaber, F X, Schmid
Publikováno v:
Journal of molecular biology. 224(1)
The folding and unfolding kinetics within the transition region were measured for RNase A and for RNase T1. The data were used to evaluate the theoretical models for the influence of prolyl isomerization on the observed folding kinetics. These two pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::2a73782bb89acafe5f2f9f7460362201
https://pubmed.ncbi.nlm.nih.gov/1548701
https://pubmed.ncbi.nlm.nih.gov/1548701
Publikováno v:
Journal of molecular biology. 224(1)
Kinetic models were developed to describe the influence of prolyl peptide bond isomerization on the kinetics of reversible protein folding for cases in which structural intermediates do not occur. In the simulations, the number of prolyl residues and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::ef47b04a64dabe7dede7b31dfdefb9a6
https://pubmed.ncbi.nlm.nih.gov/1548700
https://pubmed.ncbi.nlm.nih.gov/1548700
Autor:
B. Heinz, B. Schmidt, C. Root, H. Satzger, F. Milota, B. Fierz, T. Kiefhaber, W. Zinth, P. Gilch
Publikováno v:
Physical Chemistry Chemical Physics (PCCP); Jul2006, Vol. 8 Issue 29, p3432-3439, 8p