id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-004890-fob5lk2m	Fischbarg, J.	Predictive evidence for a porin-type β-barrel fold in CHIP28 and other members of the MIP family. A restricted-pore model common to water channels and facilitators	1995		.txt	text/plain	4800	338	68	Figure la shows a multiple-sequence alignment of nine proteins of the MIP family, namely: (a) the major intrinsic protein of the lens (MIP26) (Pisano & Chepelinsky, 1991) ; (b) soybean nodulin 26 (NOD26) (Sandal & Marcker, 1988) ; (c) glycerol facilitator (GLP) (Muramatsu & Mizuno, 1989) ; (d) Drosophila big brain (BIB) (Rao, Jan & Jan, 1990) ; (e) the vacuolar membrane pro-tein (7-TIP) (Maurel et al., 1993 ); (f) the frog aquaporin (FA-CHIP) (Abrami et al,, 1994) ; (g) the proximal tubule water channel (CHIP28k) (Zhang et al., 1993a) ; (h) the collecting duct water channel (WCH-CD1) (Fushimi et al., 1993) ; and (i) the erythrocyte water channel (CHIP28) (Preston & Agre, 1991) . In Fig. 3b , the CFPp marks and the PHD predictions delimit consistent segments which are generally once more too short to span the membrane as o~-helices. Since the structured transmembrane segments we predict are too short to be a-helices but have the correct length for [3-strands, we favor a [3-barrel fold for CHIP28.	./cache/cord-004890-fob5lk2m.txt	./txt/cord-004890-fob5lk2m.txt