Sentence examples for protein closure from inspiring English sources

The magnitude of the apparent rate constant for chemical exchange, k(exch)′, depends to some extent on the environment of the specific amide bond undergoing exchange and primarily on reaction pH, with pseudo-first-order constants of ca. 1 10 s–1 at pH 7. At this pH, k(exch)′ is generally slower than the rate of protein closure, with k(close) in the range of 10 10 s 1.

Protein Loop Closure Using Orientational Restraints from NMR Data.

Compromised gap junction coupling may arise from: 1) decreased expression of the major ventricular gap junction protein Cx43; 2) closure or reduced conductance of the gap junction channels (e.g. by altered phosphorylation state); or 3) loss of gap junctional channels from the intercalated discs.

Despite these limitations, the fact remains that, for some proteins, domain closure occurs through a simple 'pacman' opening-closing movement, whereas for others the movement is more complex with the two domains remaining in contact during the domain movement.

Classification of pY events based on cellular biological processes yielded four major categories: 1) signaling proteins in CNS development (101 pY events on 44 proteins), 2) dorsal closure (65 pY events on 11 proteins), 3) cell polarity (29 pY events on 19 proteins) and 4) Ras-interacting proteins that included REF and GEFs (22 pY events on 18 proteins).

Recently HupBMtb ortholog in M. smegmatis has been shown to possess DNA end joining/ring closure protein activity [19].

This lipid conjugation forms the autophagic double-membrane-associated LC3-II protein allowing the closure of the autophagic vacuole [ 14, 15].

The domain movement in citrate synthase is also an example of a protein that undergoes closure (84%) via hinge bending, but one that preserves some part of the domain interface.

Moreover, the critical period for the alterations of transmitter turnover seen here corresponds precisely to that identified previously for the protein biomarkers, with closure of the window of vulnerability by the second postnatal week.

Our structural results suggest mechanisms for inter-ring-negative cooperativity, intra-ring-positive cooperativity, and protein-folding chamber closure of TRiC.

For sidechain-sidechain, sidechain-backbone and backbone-backbone hydrogen bonds in proteins, tensegrity balance ("closure") is required over the entire length of the polypeptide chain that defines individually folding units in globular proteins ("domains") as well as within the repeating elements in fibrous proteins that consist of extended chain structures.