{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T01:18:20Z","timestamp":1791076700263,"version":"4.1.0"},"reference-count":41,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2009,1,1]],"date-time":"2009-01-01T00:00:00Z","timestamp":1230768000000},"content-version":"vor","delay-in-days":2041,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[2003,6]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>It was established previously that helical propensities of different amino acid residues in the middle of \u03b1\u2010helix in peptides and in proteins are very similar. The statistical analysis of the protein helices from the known three\u2010dimensional structures shows no difference in the frequency of noncharged residues in the middle and at the C terminus. Yet, experimental studies show distinctive differences for the helical propensities of noncharged residues in the middle and in the C terminus in model peptides. Is this a general effect, and is it applicable to protein helices or is it specific to the model alanine\u2010based peptides? To answer this question, the effects of substitutions at positions 28 (middle residue) and 32 (C2 position at the C terminus) of the \u03b1\u2010helix of ubiquitin on the stability of this protein are measured by using differential scanning calorimetry. The two data sets produce similar values for intrinsic helix propensity, leading to a conclusion that noncharged amino acid residues at the solvent\u2010exposed positions in the middle and at the C terminus of the \u03b1\u2010helix have the same helical propensity. This conclusion is further supported with an excellent correlation between the helix propensity scale obtained for the two positions in ubiquitin with the experimental helix propensity scale established previously and with the statistical distribution of the residues in protein helices.<\/jats:p>","DOI":"10.1110\/ps.0304303","type":"journal-article","created":{"date-parts":[[2003,5,21]],"date-time":"2003-05-21T17:32:53Z","timestamp":1053538373000},"page":"1169-1176","source":"Crossref","is-referenced-by-count":31,"title":["Noncharged amino acid residues at the solvent\u2010exposed positions in the middle and at the C terminus of the \u03b1\u2010helix have the same helical propensity"],"prefix":"10.1002","volume":"12","author":[{"given":"Dmitri N.","family":"Ermolenko","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John M.","family":"Richardson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"George I.","family":"Makhatadze","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2009,1]]},"reference":[{"key":"e_1_2_7_2_1","doi-asserted-by":"publisher","DOI":"10.1002\/pro.5560070103"},{"key":"e_1_2_7_3_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.8178170"},{"key":"e_1_2_7_4_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.8503008"},{"key":"e_1_2_7_5_1","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.1994.1016"},{"key":"e_1_2_7_6_1","doi-asserted-by":"publisher","DOI":"10.1002\/bip.1975.360140118"},{"key":"e_1_2_7_7_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M011026200"},{"key":"e_1_2_7_8_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0065-3233(08)60334-4"},{"key":"e_1_2_7_9_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0301-4622(02)00170-9"},{"key":"e_1_2_7_10_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0022-2836(02)00734-9"},{"key":"e_1_2_7_11_1","doi-asserted-by":"publisher","DOI":"10.1038\/273443a0"},{"key":"e_1_2_7_12_1","doi-asserted-by":"publisher","DOI":"10.1016\/0022-2836(92)90907-2"},{"key":"e_1_2_7_13_1","doi-asserted-by":"publisher","DOI":"10.1002\/(SICI)1097-0134(19980601)31:4<460::AID-PROT12>3.0.CO;2-D"},{"key":"e_1_2_7_14_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0022-2836(02)00465-5"},{"key":"e_1_2_7_15_1","first-page":"113","article-title":"Differential scanning calorimetry","volume":"173","author":"Lopez M.M.","year":"2002","journal-title":"Methods Mol. 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