PROTEIN ENGINEERING WITH NONCODED AMINO ACIDS: APPLICATIONS TO HIRUDIN Vincenzo De Filippis University of Padova, Padova, Italy Chapter Contents 9.1 Introduction 1226 9.2 Hirudin–Thrombin Interaction 1227 9.3 Selection of Amino Acid Replacements 1229 9.3.1 Val1 1229 9.3.2 Ser2 1230 9.3.3 Tyr3 1230 9.4 Structure-Activity Relationships 1230 9.4.1 Val1→X 1231 9.4.2 Ser2→X 1232 9.4.3 Tyr3→X: Effect of Side-Chain Volume and Hydrophobicity 1232 9.4.4 Tyr3→X: Orientation Effects 1232 9.4.5 Tyr3→X: Electronic Effects 1235 9.5 Cumulative Amino Acid Substitutions in Hirudin Yield a Highly Potent Thrombin Inhibitor 1238 9.6 Structural Mapping of Thrombin Recognition Sites in the Na-Bound and Na-Free Form 1239 9.7 Incorporation of Noncoded Amino Acids as Spectroscopic Probes in the Study of Protein Folding and Binding 1242 9.7.1 7-Azatryptophan 1243 9.7.2 3-Nitrotyrosine 1248 9.8 Concluding Remarks 1253 Acknowledgment 1254 References 1254
Protein Engineering with Noncoded Amino Acids: Applications to Hirudin
DE FILIPPIS, VINCENZO
2007
Abstract
PROTEIN ENGINEERING WITH NONCODED AMINO ACIDS: APPLICATIONS TO HIRUDIN Vincenzo De Filippis University of Padova, Padova, Italy Chapter Contents 9.1 Introduction 1226 9.2 Hirudin–Thrombin Interaction 1227 9.3 Selection of Amino Acid Replacements 1229 9.3.1 Val1 1229 9.3.2 Ser2 1230 9.3.3 Tyr3 1230 9.4 Structure-Activity Relationships 1230 9.4.1 Val1→X 1231 9.4.2 Ser2→X 1232 9.4.3 Tyr3→X: Effect of Side-Chain Volume and Hydrophobicity 1232 9.4.4 Tyr3→X: Orientation Effects 1232 9.4.5 Tyr3→X: Electronic Effects 1235 9.5 Cumulative Amino Acid Substitutions in Hirudin Yield a Highly Potent Thrombin Inhibitor 1238 9.6 Structural Mapping of Thrombin Recognition Sites in the Na-Bound and Na-Free Form 1239 9.7 Incorporation of Noncoded Amino Acids as Spectroscopic Probes in the Study of Protein Folding and Binding 1242 9.7.1 7-Azatryptophan 1243 9.7.2 3-Nitrotyrosine 1248 9.8 Concluding Remarks 1253 Acknowledgment 1254 References 1254
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