作者: Vladimir N. Uversky , Anthony L. Fink
DOI: 10.1016/S0014-5793(02)02441-9
关键词: Biophysics 、 Phi value analysis 、 Protein folding 、 Downhill folding 、 Crystallography 、 Hydrophobic collapse 、 Chemistry 、 Contact order 、 Folding funnel 、 Lattice protein 、 Folding (chemistry)
摘要: What is the first step in protein folding - hydrophobic collapse (compaction) or secondary structure formation? It still not clear if major driving force hydrogen bonding interactions both. We analyzed data on conformational characteristics of 41 globular proteins native and partially folded states. Our analysis shows that a good correlation exists between relative decrease hydrodynamic volume increase content. No compact equilibrium intermediates lacking structure, highly ordered non-compact species, were found. This provides experimental support for hypothesis occurs simultaneously with formation early stages folding.