Predicting the helix packing of globular proteins by self-correcting distance geometry.
A new self-correcting distance geometry method for predicting the three-dimensional structure of small globular proteins was assessed with a test set of 8 helical proteins. With the knowledge of the amino acid sequence and the helical segments, our completely automated method calculated the correct backbone topology of six proteins. The accuracy of the predicted structures ranged from 2.3 A to 3.1 A for the helical segments compared to the experimentally determined structures. For two proteins, the predicted constraints were not restrictive enough to yield a conclusive prediction. The method can be applied to all small globular proteins, provided the secondary structure is known from NMR analysis or can be predicted with high reliability.
Mumenthaler
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Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule-Hönggerberg, Zürich, Switzerland.
Braun
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D000595:Amino Acid Sequence; D064026:Calbindins; D003196:Computer Graphics; D018360:Crystallography, X-Ray; D016208:Databases, Factual; D006422:Hemerythrin / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D015394:Molecular Structure; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D064030:S100 Calcium Binding Protein G / Q000737:chemistry; D012984:Software
D064026:Calbindins; D006422:Hemerythrin; D011506:Proteins; D064030:S100 Calcium Binding Protein G