Topography Prediction of Helical Transmembrane Proteins by a New Modification of the Sliding Window Method

Table 2

Comparison of TMD boundaries calculated upon processing of hydrophobicity functions 𝑓_𝑛(𝑘) at 𝑛=3,4,5 on 𝐻_𝑁(𝑖) (𝑁=3 and 5) scales for GPCRs with known data from [21].

Protein name, code, length	Data source	Number and boundaries of transmembrane domains
	Scale level	1	2	3	4	5	6	7
GLR_; HUMAN P47871; 477 aa	[21, 22]	137–161	174–198	226–249	264–285	304–326	351–369	382–402
	𝐻5(𝑖),𝑛=4; 𝑢=0.266	143–166	180–192	218–257	261–288	303–327	353–368	384–401
CRFR1_; HUMAN P34998; 444 aa	[21, 23]	112–142	179–203	219–247	255–282	299–324	336–360	368–397
	𝐻3(𝑖),𝑛=5; ⟨𝑢⟩=−0.052	116–146	178–204	217–247	255–280	302–325	344–362	370–397
ADRB1_; MELGA P07700; 483 aa	[21, 24]	39–67	77–103	116–137	156–179	206–231	286–315	321–343
	𝐻3(𝑖),𝑛=4,; 𝑢=0.1	44–64	81–99	108–138	160–181	214–229	293–314	320–331
5HT1B_; HUMAN P28222; 390 aa	[21, 25]	50–75	85–110	124–145	166–187	206–228	316–336	350–371
	𝐻5(𝑖),𝑛=4; 𝑢=0.243	46–72	86–109	119–145	168–185	205–230	316–340	343–369
	𝐻5(𝑖),𝑛=3; ⟨𝑢⟩=0.182	45–73	85–110	118–145	168–185	205–229	316–340	344–370
5HT2B_; HUMAN P41595; 481 aa	[21, 26]	57–79	91–113	130–151	172–192	217–239	325–345	361–382
	𝐻5(𝑖),𝑛=5; ⟨𝑢⟩=0.164	54–81	89–; 89–109	−151; 131–151	173–194	215–243	325–352	356–381