Brandon/Hill selected list of print books and journals for the small medical library*

After thirty-six years of biennial updates, the authors take great pride in being able to publish the nineteenth version (2001) of the “Brandon/Hill Selected List of Print Books and Journals for the Small Medical Library.” This list of 630 books and 143 journals is intended as a selection guide for health sciences libraries or similar facilities. It can also function as a core collection for a library consortium. Books and journals are categorized by subject; the book list is followed by an author/editor index, and the subject list of journals, by an alphabetical title listing. Due to continuing requests from librarians, a “minimal core list” consisting of 81 titles has been pulled out from the 217 asterisked (*) initial-purchase books and marked with daggers (†*) before the asterisks. To purchase the entire collection of 630 books and to pay for 143 2001 journal subscriptions would require $124,000. The cost of only the asterisked items, books and journals, totals $55,000. The “minimal core list” book collection costs approximately $14,300.

Brandon/Hill selected list of print books and journals in allied health*

This list of 424 books and 77 journals is intended as a selection guide for print literature to be used in a library supporting allied health educational programs or allied health personnel in either an academic or health care setting. Because of the impossibility of covering the large number and wide variety of allied health professions and occupations, the recommended publications are focused primarily on the educational programs listed and recognized by the American Medical Association and other accrediting bodies. Books and journals are categorized by subject; the book list is followed by an author/editor index, and the subject list of journals by an alphabetical title listing. Items suggested for initial purchase (167 books and 31 journals) are indicated by asterisks. To purchase the entire collection of books and journals (2000 subscriptions) would require an expenditure of about $31,970. The cost of only the asterisked items totals $12,515.

Barriers to protein folding: formation of buried polar interactions is a slow step in acquisition of structure.

In the MYL mutant of the Arc repressor dimer, sets of partially buried salt-bridge and hydrogen-bond interactions mediated by Arg-31, Glu-36, and Arg-40 in each subunit are replaced by hydrophobic interactions between Met-31, Tyr-36, and Leu-40. The MYL refolding/dimerization reaction differs from that of wild type in being 10- to 1250-fold faster, having an earlier transition state, and depending upon viscosity but not ionic strength. Formation of the wild-type salt bridges in a hydrophobic environment clearly imposes a kinetic barrier to folding, which can be lowered by high salt concentrations. The changes in the position of the transition state and viscosity dependence can be explained if denatured monomers interact to form a partially folded dimeric intermediate, which then continues folding to form the native dimer. The second step is postulated to be rate limiting for wild type. Replacing the salt bridge with hydrophobic interactions lowers this barrier for MYL. This makes the first kinetic barrier rate limiting for MYL refolding and creates a downhill free-energy landscape in which most molecules which reach the intermediate state continue to form native dimers.

Residue replacements of buried aspartyl and related residues in sensory rhodopsin I: D201N produces inverted phototaxis signals.

Residue replacements were made at five positions (Arg-73, Asp-76, Tyr-87, Asp-106, and Asp-201) in the Halobacterium salinarium phototaxis receptor sensory rhodopsin I (SR-I) by site-specific mutagenesis. The sites were chosen for their correspondence in position to residues of functional importance in the homologous light-driven proton pump bacteriorhodopsin found in the same organism. This work identifies a residue in SR-I shown to be of vital importance to its attractant signaling function: Asp-201. The effect of the substitution with the isosteric asparagine is to convert the normally attractant signal of orange light stimulation to a repellent signal. In contrast, similar neutral substitution of the four other ionizable residues near the photoactive site allows essentially normal attractant and repellent phototaxis signaling. Wild-type two-photon repellent signaling by the receptor is intact in the Asp-201 mutant, genetically separating the wild-type attractant and repellent signal generation processes. A possible explanation and implications of the inverted signaling are discussed. Results of neutral residue substitution for Asp-76 confirm our previous evidence that proton transfer reactions involving this residue are not important to phototaxis but that Asp-76 functions as the Schiff base proton acceptor in proton translocation by transducer-free SR-I.