C
Clay Bracken
Researcher at Cornell University
Publications - 39
Citations - 2728
Clay Bracken is an academic researcher from Cornell University. The author has contributed to research in topics: Protein structure & Folding (chemistry). The author has an hindex of 22, co-authored 37 publications receiving 2440 citations. Previous affiliations of Clay Bracken include National Semiconductor & Columbia University.
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Journal ArticleDOI
A method for efficient isotopic labeling of recombinant proteins.
TL;DR: A rapid and efficient approach for preparing isotopically labeled recombinant proteins is presented and expression yields obtained provide a fourfold to eightfold reduction in isotope costs using simple shake flask growths.
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Targeting mitochondrial cardiolipin and the cytochrome c/cardiolipin complex to promote electron transport and optimize mitochondrial ATP synthesis
TL;DR: SS‐31 (D‐Arg‐dimethylTyr‐Lys‐Phe‐NH2) selectively binds to cardiolipin and inhibits cytochrome c peroxidase activity, and it is examined whether SS‐31 also protected the electron carrier function of cy tochrome c.
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Temperature dependence of intramolecular dynamics of the basic leucine zipper of GCN4: implications for the entropy of association with DNA
TL;DR: Results suggest that, for the basic region, lowering the temperature increases the population of transient helical conformations, and concomitantly reduces the amplitude or timescale of conformational fluctuations on picosecond-nanosecond timescales.
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Val66Met polymorphism of BDNF alters prodomain structure to induce neuronal growth cone retraction.
Agustin Anastasia,Katrin Deinhardt,Katrin Deinhardt,Moses V. Chao,Nathan E. Will,Krithi Irmady,Francis S. Lee,Barbara L. Hempstead,Clay Bracken +8 more
TL;DR: It is shown that the isolated BDNF prodomain is detected in the hippocampus and that it can be secreted from neurons in an activity-dependent manner and identifies the Met66 prodomain as a new active ligand which modulates neuronal morphology.
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An effective method for the discrimination of motional anisotropy and chemical exchange.
TL;DR: This analysis provides a simple method for rapidly estimating and dissociating the effects of motional anisotropy and chemical exchange in NMR heteronuclear spin relaxation data and demonstrates the utility of the method with 15N relaxation data collected on the proteins E. coli ribonuclease H and the trimeric E coli membrane associated lipoprotein lpp.