Publications

Lane, Todd L.; Lane, Pamela L.; Carney, Laura T.; Solberg, Owen D.; Williams, Kelly P.

Abstract not provided.

Branda, Steven B.; Jebrail, Mais J.; Van De Vreugde, James L.; Langevin, Stanley A.; Bent, Zachary B.; Curtis, Deanna J.; Lane, Pamela L.; Carson, Bryan C.; La Bauve, Elisa L.; Patel, Kamlesh P.; Ricken, James B.; Schoeniger, Joseph S.; Solberg, Owen D.; Williams, Kelly P.; Misra, Milind; Powell, Amy J.; Pattengale, Nicholas D.; May, Elebeoba E.; Lane, Todd L.; Lindner, Duane L.; Young, Malin M.; VanderNoot, Victoria A.; Thaitrong, Numrin T.; Bartsch, Michael B.; Renzi, Ronald F.; Tran-Gyamfi, Mary B.; Meagher, Robert M.

Abstract not provided.

Branda, Steven B.; Jebrail, Mais J.; Van De Vreugde, James L.; Langevin, Stanley A.; Bent, Zachary B.; Curtis, Deanna J.; Lane, Pamela L.; Carson, Bryan C.; La Bauve, Elisa L.; Patel, Kamlesh P.; Ricken, James B.; Schoeniger, Joseph S.; Solberg, Owen D.; Williams, Kelly P.; Misra, Milind; Powell, Amy J.; Pattengale, Nicholas D.; May, Elebeoba E.; Lane, Todd L.; Lindner, Duane L.; Young, Malin M.; VanderNoot, Victoria A.; Thaitrong, Numrin T.; Bartsch, Michael B.; Renzi, Ronald F.; Tran-Gyamfi, Mary B.; Meagher, Robert M.

Abstract not provided.

Langevin, Stanley A.; Bent, Zachary B.; Solberg, Owen D.; Curtis, Deanna J.; Lane, Pamela L.; Williams, Kelly P.; Schoeniger, Joseph S.; Lane, Todd L.; Branda, Steven B.

Abstract not provided.

Langevin, Stanley A.; VanderNoot, Victoria A.; Solberg, Owen D.; Curtis, Deanna J.; Tran-Gyamfi, Mary B.; Lane, Pamela L.; Branda, Steven B.; Lane, Todd L.

Abstract not provided.

Nucleic Acid Research

Langevin, Stanley A.; Lane, Todd L.; Lane, Pamela L.; Bent, Zachary B.; Solberg, Owen D.; Curtis, Deanna J.; Williams, Kelly P.; Branda, Steven B.; Patel, Kamlesh P.; Schoeniger, Joseph S.

Abstract not provided.

Williams, Kelly P.; Curtis, Deanna J.; Lane, Pamela L.; Lane, Todd L.

Abstract not provided.

Lane, Pamela L.; Lane, Todd L.; Zendejas, Frank Z.

The purpose of this LDRD was to generate data that could be used to populate and thereby reduce the uncertainty in global carbon cycle models. These efforts were focused on developing a system for determining the dissolution rate of biogenic calcite under oceanic pressure and temperature conditions and on carrying out a digital transcriptomic analysis of gene expression in response to changes in pCO2, and the consequent acidification of the growth medium.

Chemometrics and Intelligent Laboratory Systems

Van Benthem, Mark V.; Lane, Todd L.; Davis, Ryan W.; Lane, Pamela L.

Abstract not provided.

Proposed for publication in Analytical Chemistry.

Lane, Todd L.; Lane, Pamela L.; Branda, Steven B.; VanderNoot, Victoria A.

Abstract not provided.

Powell, Amy J.; Davis, Ryan W.; Lane, Todd L.; Lane, Pamela L.; Keenan, Michael R.; Van Benthem, Mark V.

This short-term, late-start LDRD examined the effects of nutritional deprivation on the energy harvesting complex in microalgae. While the original experimental plan involved a much more detailed study of temperature and nutrition on the antenna system of a variety of TAG producing algae and their concomitant effects on oil production, time and fiscal constraints limited the scope of the study. This work was a joint effort between research teams at Sandia National Laboratories, New Mexico and California. Preliminary results indicate there is a photosystem response to silica starvation in diatoms that could impact the mechanisms for lipid accumulation.

Lane, Todd L.; Lane, Pamela L.

Abstract not provided.

Yu, Eizadora T.; Lane, Pamela L.; Lane, Todd L.; Zendejas, Frank Z.; Simmons, Blake S.

Abstract not provided.

Lane, Todd L.; Lane, Pamela L.; Curtis, Deanna J.

Abstract not provided.

Yu, Eizadora T.; Lane, Todd L.; Lane, Pamela L.; Simmons, Blake S.; Zendejas, Frank Z.

Abstract not provided.

Juarez, Cindy J.; Zendejas, Frank Z.; Simmons, Blake S.; Gaucher, Sara P.; Lane, Pamela L.; Lane, Todd L.

Abstract not provided.

Schoeniger, Joseph S.; Ayson, Marites J.; Jacobsen, Rick B.; Lane, Pamela L.; Sale, Kenneth L.; Young, Malin M.

Membrane proteins make up a diverse and important subset of proteins for which structural information is limited. In this study, chemical cross-linking and mass spectrometry were used to explore the structure of the G-protein-coupled photoreceptor bovine rhodopsin in the dark-state conformation. All experiments were performed in rod outer segment membranes using amino acid 'handles' in the native protein sequence and thus minimizing perturbations to the native protein structure. Cysteine and lysine residues were covalently cross-linked using commercially available reagents with a range of linker arm lengths. Following chemical digestion of cross-linked protein, cross-linked peptides were identified by accurate mass measurement using liquid chromatography-fourier transform mass spectrometry and an automated data analysis pipeline. Assignments were confirmed and, if necessary, resolved, by tandem MS. The relative reactivity of lysine residues participating in cross-links was evaluated by labeling with NHS-esters. A distinct pattern of cross-link formation within the C-terminal domain, and between loop I and the C-terminal domain, emerged. Theoretical distances based on cross-linking were compared to inter-atomic distances determined from the energy-minimized X-ray crystal structure and Monte Carlo conformational search procedures. In general, the observed cross-links can be explained by re-positioning participating side-chains without significantly altering backbone structure. One exception, between C3 16 and K325, requires backbone motion to bring the reactive atoms into sufficient proximity for cross-linking. Evidence from other studies suggests that residues around K325 for a region of high backbone mobility. These findings show that cross-linking studies can provide insight into the structural dynamics of membrane proteins in their native environment.