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Titolo:
Environmentally induced reversible conformational switching in the yeast cell adhesion protein alpha-agglutinin
Autore:
Zhao, H; Chen, MH; Shen, ZM; Kahn, PC; Lipke, PN;
Indirizzi:
CUNY Hunter Coll, Dept Sci Biol, New York, NY 10021 USA CUNY Hunter Coll New York NY USA 10021 t Sci Biol, New York, NY 10021 USA CUNY Hunter Coll, Inst Biomol Struct & Funct, New York, NY 10021 USA CUNY Hunter Coll New York NY USA 10021 ct & Funct, New York, NY 10021 USA Rutgers State Univ, Cook Coll, Dept Biochem & Microbiol, New Brunswick, NJ08901 USA Rutgers State Univ New Brunswick NJ USA 08901 New Brunswick, NJ08901 USA
Titolo Testata:
PROTEIN SCIENCE
fascicolo: 6, volume: 10, anno: 2001,
pagine: 1113 - 1123
SICI:
0961-8368(200106)10:6<1113:EIRCSI>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
CIRCULAR-DICHROISM SPECTROSCOPY; SECONDARY STRUCTURE PREDICTION; AMINO-ACID-SEQUENCE; BETA-SHEET PROTEIN; SACCHAROMYCES-CEREVISIAE; IMMUNOGLOBULIN SUPERFAMILY; INFLUENZA HEMAGGLUTININ; SEXUAL AGGLUTINATION; PEPTIDE; LACTOGLOBULIN;
Keywords:
cell adhesion protein; circular dichroism; conformational shift; glycoprotein; peptide conformation; secondary structure prediction;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
59
Recensione:
Indirizzi per estratti:
Indirizzo: Lipke, PN CUNY Hunter Coll, Dept Sci Biol, 695 Pk Ave, New York, NY 10021 USA CUNY Hunter Coll 695 Pk Ave New York NY USA 10021 , NY 10021 USA
Citazione:
H. Zhao et al., "Environmentally induced reversible conformational switching in the yeast cell adhesion protein alpha-agglutinin", PROTEIN SCI, 10(6), 2001, pp. 1113-1123

Abstract

The yeast cell adhesion protein cr-agglutinin is expressed on the surface of a free-living organism and is subjected to a variety of environmental conditions. Circular dichroism (CD) spectroscopy shows that the binding region of alpha -agglutinin has a beta -sheet-rich structure, with only similar to2% alpha -helix under native conditions (15-40 degreesC at pH 5.5). This region is predicted to fold into three immunoglobulin-like domains, and models are consistent with the CD spectra as well as with peptide mapping and site-specific mutagenesis. However, secondary structure prediction algorithms show that segments comprising similar to 17% of the residues have high alpha -helical and low beta -sheet potential. Two model peptides of such segments had helical tendencies, and one of these peptides showed pH-dependentconformational switching. Similarly, CD spectroscopy of the binding regionof alpha -agglutinin showed reversible conversion from beta -rich to mixedalpha/beta structure at elevated temperatures or when the pH was changed. The reversibility of these changes implied that there is a small energy difference between the all-beta and the alpha/beta states. Similar changes followed cleavage of peptide or disulfide bonds. Together, these observations imply that short sequences of high helical propensity are constrained to a beta -rich state by covalent and local charge interactions under native conditions, but form helices under non-native conditions.

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Documento generato il 25/09/20 alle ore 21:35:20