Protein Science

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The ankyrin repeat as molecular architecture for protein recognition
Protein Science - Tập 13 Số 6 - Trang 1435-1448 - 2004
Leila K Mosavi, Tobin J. Cammett, Daniel C. Desrosiers, Z Y Peng
AbstractThe ankyrin repeat is one of the most frequently observed amino acid motifs in protein databases. This protein–protein interaction module is involved in a diverse set of cellular functions, and consequently, defects in ankyrin repeat proteins have been found in a number of human diseases. Recent biophysical, crystallographic, and NMR studies have been used ...... hiện toàn bộ
Helix‐bundle membrane protein fold templates
Protein Science - Tập 8 Số 12 - Trang 2711-2719 - 1999
James U. Bowie
AbstractIn the fold recognition approach to structure prediction, a sequence is tested for compatibility with an already known fold. For membrane proteins, however, few folds have been determined experimentally. Here the feasibility of computing the vast majority of likely membrane protein folds is tested. The results indicate that conformation space can be effecti...... hiện toàn bộ
Structure of the transmembrane region of the M2 protein H+ channel
Protein Science - Tập 10 Số 11 - Trang 2241-2250 - 2001
Junfeng Wang, Sanguk Kim, Frank Kovacs, Timothy A. Cross
AbstractThe transmembrane domain of the M2 protein from influenza A virus forms a nearly uniform and ideal helix in a liquid crystalline bilayer environment. The exposure of the hydrophilic backbone structure is minimized through uniform hydrogen bond geometry imposed by the low dielectric lipid environment. A high‐resolution structure of the monomer backbone and a...... hiện toàn bộ
The structure of human pancreaticα-amylase at 1.8 Å resolution and comparisons with related enzymes
Protein Science - Tập 4 Số 9 - Trang 1730-1742 - 1995
Gary D. Brayer, Yaoguang Luo, Stephen G. Withers
Structure of a pancreatic α‐amylase bound to a substrate analogue at 2.03 Å resolution
Protein Science - Tập 6 Số 11 - Trang 2285-2296 - 1997
Mingxing Qian, S. Spinelli, F. Payan
AbstractThe structure of pig pancreatic α‐amylase in complex with carbohydrate inhibitor and proteinaceous inhibitors is known but the successive events occurring at the catalytic center still remain to be elucidated. The X‐ray structure analysis of a crystal of pig pancreatic α‐amylase (PPA, EC 3.2.1.1.) soaked with an enzyme‐resistant substrate analogue, methyl 4...... hiện toàn bộ
Carbohydrate binding sites in a pancreatic α‐amylase‐substrate complex, derived from X‐ray structure analysis at 2.1 Å resolution
Protein Science - Tập 4 Số 4 - Trang 747-755 - 1995
Minxie Qian, Richard Haser, F. Payan
AbstractThe X‐ray structure analysis of a crystal of pig pancreatic α‐amylase (PPA, EC 3.2.1.1.) that was soaked with the substrate maltopentaose showed electron density corresponding to two independent carbohydrate recognition sites on the surface of the molecule. Both binding sites are distinct from the active site described in detail in our previous high‐resolut...... hiện toàn bộ
Estimation of the number of α‐helical and β‐strand segments in proteins using circular dichroism spectroscopy
Protein Science - Tập 8 Số 2 - Trang 370-380 - 1999
Narasimha Sreerama, S.Yu. Venyaminov, Robert W. Woody
AbstractA simple approach to estimate the number of α‐helical and β‐strand segments from protein circular dichroism spectra is described. The α‐helix and β‐sheet conformations in globular protein structures, assigned by DSSP and STRIDE algorithms, were divided into regular and distorted fractions by considering a certain number of terminal residues in a given α‐hel...... hiện toàn bộ
Outer membrane protein A of E. coli folds into detergent micelles, but not in the presence of monomeric detergent
Protein Science - Tập 8 Số 10 - Trang 2065-2071 - 1999
Jörg H. Kleinschmidt, Michael C. Wiener, Lukas K. Tamm
AbstractOuter membrane protein A (OmpA) of Escherichia coli is a β‐barrel membrane protein that unfolds in 8 M urea to a random coil. OmpA refolds upon urea dilution in the presence of certain detergents or lipids. To examine the minimal requirements for secondary and tertiary structure formation in β‐barrel membrane proteins, folding of ...... hiện toàn bộ
Crystal structure of Saccharomyces cerevisiae cytosolic aspartate aminotransferase
Protein Science - Tập 7 Số 6 - Trang 1380-1387 - 1998
Constance J. Jeffery, Gregory A. Petsko, Dagmar Ringe, T. N. Barry, Shawn Doonan
AbstractThe crystal structure of Saccharomyces cerevisiae cytoplasmic aspartate aminotransferase (EC 2.6.1.1) has been determined to 2.05 Å resolution in the presence of the cofactor pyridoxal‐5′‐phosphate and the competitive inhibitor maleate. The structure was solved by the method of molecular replacement. The final value of the crystal...... hiện toàn bộ
Motifs and structural fold of the cofactor binding site of human glutamate decarboxylase
Protein Science - Tập 7 Số 5 - Trang 1092-1105 - 1998
Kunbin Qu, David L. Martin, Charles E. Lawrence
AbstractThe pyridoxal‐P binding sites of the two isoforms of human glutamate decarboxylase (GAD65 and GAD67) were modeled by using PROBE (a recently developed algorithm for multiple sequence alignment and database searching) to align the primary sequence of GAD with pyridoxal‐P binding proteins of known structure. GAD's cofactor binding site is particularly interes...... hiện toàn bộ
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