Abstract

The objective of this project continues to be the use of NMR spectroscopy to learn about the mobility and relative orientations of groups in polypeptides and proteins, and thereby determine the conformations of these molecules in solution. In some cases, the results of these experiments will be combined with those from conformational energy calculations to reduce the ambiguities present in both the spectroscopic and computational techniques. The primary aim is to solve structural problems related to biological function Various two- and three-dimensional NMR techniques are being applied to natural and synthetic polypeptides and proteins in solution. Each system is selected to answer a specific conformational question, e.g. the mechanism of folding of ribonuclease, and the structure and function of growth factors.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM024893-23
Application #
3272635
Study Section
Molecular and Cellular Biophysics Study Section (BBCA)
Project Start
1978-04-01
Project End
1996-06-30
Budget Start
1993-07-01
Budget End
1994-06-30
Support Year
23
Fiscal Year
1993
Total Cost
Indirect Cost

  Institution

Name
Cornell University
Department
Type
Schools of Arts and Sciences
DUNS #
City
Ithaca
State
NY
Country
United States
Zip Code
14850

  Publications

Vila, Jorge A (2012) Limiting values of the 15N chemical shift of the imidazole ring of histidine at high pH. J Phys Chem B 116:6665-9
Gahl, Robert F; Oswald, Robert E; Scheraga, Harold A (2012) Identification of formation of initial native structure in onconase from an unfolded state. Biochemistry 51:521-32
Vila, Jorge A; Arnautova, Yelena A; Vorobjev, Yury et al. (2011) Assessing the fractions of tautomeric forms of the imidazole ring of histidine in proteins as a function of pH. Proc Natl Acad Sci U S A 108:5602-7
Martin, Osvaldo A; Villegas, Myriam E; Vila, Jorge A et al. (2010) Analysis of 13Calpha and 13Cbeta chemical shifts of cysteine and cystine residues in proteins: a quantum chemical approach. J Biomol NMR 46:217-25
Lewandowska, Agnieszka; Oldziej, Stanislaw; Liwo, Adam et al. (2010) Mechanism of formation of the C-terminal beta-hairpin of the B3 domain of the immunoglobulin binding protein G from Streptococcus. III. Dynamics of long-range hydrophobic interactions. Proteins 78:723-37
Vila, Jorge A; Serrano, Pedro; Wüthrich, Kurt et al. (2010) Sequential nearest-neighbor effects on computed 13Calpha chemical shifts. J Biomol NMR 48:23-30
Gahl, Robert F; Pradeep, Lovy; Siegel, Corey R et al. (2009) Effects of tyrosine mutations on the conformational and oxidative folding of ribonuclease a: a comparative study. Biochemistry 48:3887-93
Vila, Jorge A; Scheraga, Harold A (2009) Assessing the accuracy of protein structures by quantum mechanical computations of 13C(alpha) chemical shifts. Acc Chem Res 42:1545-53
Vila, Jorge A; Baldoni, Héctor A; Scheraga, Harold A (2009) Performance of density functional models to reproduce observed (13)C(alpha) chemical shifts of proteins in solution. J Comput Chem 30:884-92
Vila, Jorge A; Arnautova, Yelena A; Martin, Osvaldo A et al. (2009) Quantum-mechanics-derived 13Calpha chemical shift server (CheShift) for protein structure validation. Proc Natl Acad Sci U S A 106:16972-7

Showing the most recent 10 out of 123 publications