The Hurricane Mountain Formation Melange and unconfomably overlying Lower to Middle Ordovician volcanics, Brassua Lake and Moosehead Lake Quadrangles

New England Intercollegiate Geological Conference Guidebook for field trips in The Greenville - Millinocket Regions, North Central Maine, October 7-9, 1983: Trip B-

Tectonic and Metamorphic History of the Lower Devonian Rocks in the Carrabasset Valley North of Kingfield, Maine

Guidebook for field trips in the Rangeley Lakes - Dead River Basin region, western Maine: 62nd annual meeting October 2, 3, and 4, 1970: Trip A-

Pre-Silurian Flysch Relich Relict Structures in Cordierite-K-Feldspar Granofelses, Long Falls of Dead River, Somerset County, Western Maine

Guidebook for field trips in the Rangeley Lakes - Dead River Basin region, western Maine: 62nd annual meeting October 2, 3, and 4, 1970: Trip B-

The Chain Lakes Massif and its Contact With a Cambrian Ophiolite and a Caradocian Granite

Guidebook for field trips in southern and west-central Maine, October 13, 14 and 15, 1989: New England Intercollegiate Geological Conference 81st annual meeting: Trip B-

The Chain Lakes Massif and its Contact With a Cambrian Ophiolite and a Caradocian Granite

Guidebook for field trips in southern and west-central Maine, October 13, 14 and 15, 1989: New England Intercollegiate Geological Conference 81st annual meeting: Trip A-

Guidebook for field trips in the Rangeley Lakes - Dead River Basin region, western Maine: 62nd annual meeting October 2, 3, and 4, 1970

Geologic fieldtrips in Main

Bedrock geology of the Rangeley Lakes-Dead River basin region, western Maine

Guidebook for field trips in the Rangeley Lakes - Dead River Basin region, western Maine: 62nd annual meeting October 2, 3, and 4, 1970: title page, table of contents, foreword, essa

Bringing order to protein disorder through comparative genomics and genetic interactions

Abstract Background Intrinsically disordered regions are widespread, especially in proteomes of higher eukaryotes. Recently, protein disorder has been associated with a wide variety of cellular processes and has been implicated in several human diseases. Despite its apparent functional importance, the sheer range of different roles played by protein disorder often makes its exact contribution difficult to interpret. Results We attempt to better understand the different roles of disorder using a novel analysis that leverages both comparative genomics and genetic interactions. Strikingly, we find that disorder can be partitioned into three biologically distinct phenomena: regions where disorder is conserved but with quickly evolving amino acid sequences (flexible disorder); regions of conserved disorder with also highly conserved amino acid sequences (constrained disorder); and, lastly, non-conserved disorder. Flexible disorder bears many of the characteristics commonly attributed to disorder and is associated with signaling pathways and multi-functionality. Conversely, constrained disorder has markedly different functional attributes and is involved in RNA binding and protein chaperones. Finally, non-conserved disorder lacks clear functional hallmarks based on our analysis. Conclusions Our new perspective on protein disorder clarifies a variety of previous results by putting them into a systematic framework. Moreover, the clear and distinct functional association of flexible and constrained disorder will allow for new approaches and more specific algorithms for disorder detection in a functional context. Finally, in flexible disordered regions, we demonstrate clear evolutionary selection of protein disorder with little selection on primary structure, which has important implications for sequence-based studies of protein structure and evolution