Abstract

Our objective is the use of NMR to learn about the mobility and relative orientations of groups in polypeptides, and thereby determine the conformations of these molecules in solution. The results of the NMR0 experiments will be combined with those from conformational energy calculations, to reduce the ambiguities present in both techniques. NMR studies will be carried out on vasopressin, oxytocin, enkephalin, gramicidin S, actinomycin D, and on various synthetic model polypeptides, each of which is designed to answer a specific conformational question. Also EPR studies will be carried out on spin-labeled ribonuclease to determine the pathway(s) of folding of this protein from the unfolded form (both with and without the disulfide bonds intact).

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM024893-16
Application #
3272630
Study Section
Biophysics and Biophysical Chemistry B Study Section (BBCB)
Project Start
1978-04-01
Project End
1986-03-31
Budget Start
1985-04-01
Budget End
1986-03-31
Support Year
16
Fiscal Year
1985
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
Arnautova, Yelena A; Vila, Jorge A; Martin, Osvaldo A et al. (2009) What can we learn by computing 13Calpha chemical shifts for X-ray protein models? Acta Crystallogr D Biol Crystallogr 65:697-703
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

Showing the most recent 10 out of 123 publications