1. 1. Importance of water (solvent) effect on biomolecular interactions
1.1. "Water (the solvent) is a crucial factor in biomolecular interactions that is often overlooked."
1.1.1. Mention that it's definitely important for kinesin
1.1.2. And, given the crowded nature of cell, osmotic pressure in cell is important factor (can cite papers here)
1.2. Examples from other fields, especially protein-DNA
1.3. cite
1.3.1. Parsegian,Rand, Rau review (Meth Enz 1995)
1.3.1.1. I want to convey same message as these guys / I wouldn't be averse to quoting them directly
1.3.2. Sidorova and Rau protein-DNA (PNAS, Biopolymers ~1996/2000?)
1.3.3. Others
1.3.4. Fraunfelder Hydration Shell (2008?)
2. 3. Introduction to what will be in this paper
2.1. "Despite the importance, it can be argued that the solvent (water) has seen relatively little attention for the kinesin / microtubule system"
2.2. "In this paper we show": Heavy-hydrogen water (D2O) and heavy-oxygen water (H2O18) effects in gliding motility assay
2.2.1. Both isotopes showed reduction in speed
2.2.2. D2O more substantial than O18
2.2.3. We'll discuss possible mechanisms for this effect, highlighting the change in solvent viscosity as a possible explanation
2.2.4. Cite
2.2.4.1. Gliding assay (Vale 19xx, kinesin home page)
2.2.4.2. Maybe cite the viscosity paper (2010) here, definitely elsewhere in our paper of course)
2.2.4.3. I remember seeing a Hackney 0-18 paper at Biophys 2010. Not sure if published though.
2.3. I guess we never got around to repeating the MT stability (D2O) experiments. So, it's tough to say anything about it in the introduction. It would fit in well to mention that "some research groups are looking at molecular motor systems as components of microdevices. It's possible that D2O is a superior solvent for these devices due to protein stability. Thus, it's important to characterize this stability as well as the molecular behaviors in this new solvent."
3. 2. Prior molecular motor work
3.1. (This continues from above paragraph, using specific examples of water effects. Just more specific for molecular motors / MTs)
3.2. Actin/Myosin
3.2.1. Cooke Lab work (osmotic/differing sizes)
3.2.2. Highsmith D2O
3.2.3. Other?
3.3. Tubulin/MT
3.3.1. Stabilized tubulin D2O
3.3.1.1. We have a paper (or more) showing that tubulin at 4C is more stable in D2O
3.3.1.1.1. Could also go further and cite that proteins in general are more stable in D2O (there is that "experts review" paper that I have, talking about vaccines specifically). Also there is the fruit fly D2O stability
3.3.2. Promoted MT polymerization D2O
3.3.2.1. I believe there were studies of MT polymerization in D2O showing that it proceeded more quickly. we have these refs
3.3.3. Bunch of things to cite for these Actin/Mysin and Tubulin papers. Probably like 6 total.