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Stran 325
We find that the change in internal dynamics of the protein calmodulin varies significantly on binding a variety of target domains . Surprisingly , the apparent change in the corresponding conformational entropy is linearly related to ...
We find that the change in internal dynamics of the protein calmodulin varies significantly on binding a variety of target domains . Surprisingly , the apparent change in the corresponding conformational entropy is linearly related to ...
Stran 326
There are 56 methyl - bearing amino acids providing 80 methyl groups as probes distributed across the primary sequence of calmodulin and including 9 methionines that line the target domain binding sites formed in the various complexes ...
There are 56 methyl - bearing amino acids providing 80 methyl groups as probes distributed across the primary sequence of calmodulin and including 9 methionines that line the target domain binding sites formed in the various complexes ...
Stran 327
The conformational entropy of binding The simple and direct interpretation of changes in dynamics as changes in conformational entropy is model - dependent and is therefore somewhat sensitive to the underlying accuracy of the model used ...
The conformational entropy of binding The simple and direct interpretation of changes in dynamics as changes in conformational entropy is model - dependent and is therefore somewhat sensitive to the underlying accuracy of the model used ...
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Bibliografski podatki
| Naslov | Nature, Količina 448 |
| Urednik | Sir Norman Lockyer |
| Založnik | Macmillan Journals Limited, 2007 |
| Vir izvirnika | Univerza Illinois (Urbana in Champaign) |
| Pretvorjeno v digitalni zapis | 12 dec 2018 |
| Izvozi navedbo | BiBTeX EndNote RefMan |