Works matching IS 08873585 AND DT 1996 AND VI 25 AND IP 1
Results: 16
Constructing amino acid residue substitution classes maximally indicative of local protein structure.
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- Proteins, 1996, v. 25, n. 1, p. 28, doi. 10.1002/(SICI)1097-0134(199605)25:1<28::AID-PROT3>3.0.CO;2-G
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On the sensitivity of MD trajectories to changes in water-protein interaction parameters: The potato carboxypeptidase inhibitor in water as a test case for the GROMOS force field.
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- Proteins, 1996, v. 25, n. 1, p. 89, doi. 10.1002/(SICI)1097-0134(199605)25:1<89::AID-PROT7>3.0.CO;2-F
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Crystallization and preliminary crystallographic analysis of RepA1, a replication control protein of the RepFIC replicon of enterotoxin plasmid EntP307.
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- Proteins, 1996, v. 25, n. 1, p. 137, doi. 10.1002/(SICI)1097-0134(199605)25:1<137::AID-PROT13>3.0.CO;2-L
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Molecular dynamics study of phospholipase A<sub>2</sub> on a membrane surface.
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- Proteins, 1996, v. 25, n. 1, p. 12, doi. 10.1002/(SICI)1097-0134(199605)25:1<12::AID-PROT2>3.0.CO;2-M
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Study of global motions in proteins by weighted masses molecular dynamics: Adenylate kinase as a test case.
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- Proteins, 1996, v. 25, n. 1, p. 79, doi. 10.1002/(SICI)1097-0134(199605)25:1<79::AID-PROT6>3.0.CO;2-F
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Crystallization of a family 8 cellulase from Clostridium thermocellum.
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- Proteins, 1996, v. 25, n. 1, p. 134, doi. 10.1002/(SICI)1097-0134(199605)25:1<134::AID-PROT12>3.0.CO;2-L
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Prediction of the secondary structure of HIV-1 gp120.
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- Proteins, 1996, v. 25, n. 1, p. 1, doi. 10.1002/(SICI)1097-0134(199605)25:1<1::AID-PROT1>3.0.CO;2-N
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The rate-limiting step in the folding of the cis-Pro167Thr mutant of TEM-1 β-lactamase is the trans to cis isomerization of a non-proline peptide bond.
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- Proteins, 1996, v. 25, n. 1, p. 104, doi. 10.1002/(SICI)1097-0134(199605)25:1<104::AID-PROT8>3.0.CO;2-J
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Purification, stabilization, and crystallization of a modular protein: Grb2.
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- Proteins, 1996, v. 25, n. 1, p. 112, doi. 10.1002/(SICI)1097-0134(199605)25:1<112::AID-PROT9>3.0.CO;2-L
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Why are protein crystallographic R-values so high?
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- Proteins, 1996, v. 25, n. 1, p. i, doi. 10.1002/prot.340250102
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Accessing the Kabat antibody sequence database by computer.
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- Proteins, 1996, v. 25, n. 1, p. 130, doi. 10.1002/(SICI)1097-0134(199605)25:1<130::AID-PROT11>3.0.CO;2-L
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The three-dimensional structure of Escherichia coli porphobilinogen deaminase at 1.76-Å resolution.
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- Proteins, 1996, v. 25, n. 1, p. 48, doi. 10.1002/(SICI)1097-0134(199605)25:1<48::AID-PROT5>3.0.CO;2-G
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Masthead.
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- Proteins, 1996, v. 25, n. 1, p. fmi, doi. 10.1002/prot.340250101
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Molecular docking using surface complementarity.
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- Proteins, 1996, v. 25, n. 1, p. 120, doi. 10.1002/(SICI)1097-0134(199605)25:1<120::AID-PROT10>3.0.CO;2-M
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Crystallization and preliminary X-ray analysis of Escherichia coli methionyl-tRNA.
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- Proteins, 1996, v. 25, n. 1, p. 139, doi. 10.1002/(SICI)1097-0134(199605)25:1<139::AID-PROT14>3.0.CO;2-L
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Predicting solvent accessibility: Higher accuracy using Bayesian statistics and optimized residue substitution classes.
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- Proteins, 1996, v. 25, n. 1, p. 38, doi. 10.1002/(SICI)1097-0134(199605)25:1<38::AID-PROT4>3.0.CO;2-G
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