Review of the fourth Johns Hopkins Protein Folding Meeting.
- Published in:
- Proteins, 1999, v. 36, n. 3, p. 263, doi. 10.1002/(SICI)1097-0134(19990815)36:3<263::AID-PROT1>3.0.CO;2-Q
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- Article
Works matching IS 08873585 AND DT 1999 AND VI 36 AND IP 3
Results: 11
1
2
Examination of shape complementarity in docking of Unbound proteins.
- Published in:
- Proteins, 1999, v. 36, n. 3, p. 307, doi. 10.1002/(SICI)1097-0134(19990815)36:3<307::AID-PROT5>3.0.CO;2-R
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3
Evaluation of short-range interactions as secondary structure energies for protein fold and sequence recognition.
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- Proteins, 1999, v. 36, n. 3, p. 347, doi. 10.1002/(SICI)1097-0134(19990815)36:3<347::AID-PROT9>3.0.CO;2-3
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- Article
4
Mechanism of substrate dephosphorylation in low M<sub>r</sub> protein tyrosine phosphatase.
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- Proteins, 1999, v. 36, n. 3, p. 370, doi. 10.1002/(SICI)1097-0134(19990815)36:3<370::AID-PROT11>3.0.CO;2-9
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- Article
5
High resolution structure and sequence of T. aurantiacus Xylanase I: Implications for the evolution of thermostability in family 10 xylanases and enzymes with βα-barrel architecture.
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- Proteins, 1999, v. 36, n. 3, p. 295, doi. 10.1002/(SICI)1097-0134(19990815)36:3<295::AID-PROT4>3.0.CO;2-6
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6
Methodology for protein-ligand binding studies: Application to a model for drug resistance, the HIV/FIV protease system.
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- Proteins, 1999, v. 36, n. 3, p. 318, doi. 10.1002/(SICI)1097-0134(19990815)36:3<318::AID-PROT6>3.0.CO;2-K
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7
Role of evolutionary information in predicting the disulfide-bonding state of cysteine in proteins.
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- Proteins, 1999, v. 36, n. 3, p. 340, doi. 10.1002/(SICI)1097-0134(19990815)36:3<340::AID-PROT8>3.0.CO;2-D
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8
X-ray crystallographic studies of the denaturation of ribonuclease S.
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- Proteins, 1999, v. 36, n. 3, p. 282, doi. 10.1002/(SICI)1097-0134(19990815)36:3<282::AID-PROT3>3.0.CO;2-F
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9
Estimates of the loss of main-chain conformational entropy of different residues on protein folding.
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- Proteins, 1999, v. 36, n. 3, p. 332, doi. 10.1002/(SICI)1097-0134(19990815)36:3<332::AID-PROT7>3.0.CO;2-H
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10
Macromolecular impurities and disorder in protein crystals.
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- Proteins, 1999, v. 36, n. 3, p. 270, doi. 10.1002/(SICI)1097-0134(19990815)36:3<270::AID-PROT2>3.0.CO;2-N
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11
An empirical energy potential with a reference state for protein fold and sequence recognition.
- Published in:
- Proteins, 1999, v. 36, n. 3, p. 357, doi. 10.1002/(SICI)1097-0134(19990815)36:3<357::AID-PROT10>3.0.CO;2-U
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- Article