New theoretical approach for elucidating the solution structure of peptides from NMR data. Final report on DOE Grant DE-FG02-97ER62490

Meirovitch, Hagai

Florida State University, Tallahassee, FL (United States)

关键词: Dna;    Crystallography;    Carbohydrates;    Statistical Mechanics;    59 Basic Biological Sciences;   

DOI  :  10.2172/771251
RP-ID  :  NONE
RP-ID  :  FG02-97ER62490
RP-ID  :  771251

美国|英语

来源: UNT Digital Library

【 摘 要 】

In this project we have developed a new computational methodology, based on statistical mechanics considerations, for analyzing experimental structural data of flexible peptides and segments of proteins (typically surface loops and chain ends). This methodology is applicable to multidimensional nuclear magnetic resonance (NMR), X-ray crystallography, and potentially fluorescence spectroscopy and other techniques. NMR is the only physical technique that can generate three dimensional structures of biomolecules in solution. It is well established for globular proteins which reside in a single microstate, i.e. a limited region of conformational space around the native structure. Nuclear Overhauser Enhancement (NOE) contacts indicative of structure can also be obtained from more flexible systems (e.g., peptides, carbohydrates, and DNA segments), which are expected to populate significantly several microstates in thermodynamic equilibrium. However, in this case the NOEs might become weighted averages of contributions of the individual microstates, which makes the interpretation of the data difficult, because of the need to identify the most stable microstates arid calculate their relative populations. Development of reliable analysis techniques in this field is a challenge.