Related ArticlesInvestigation of the solution structure of chymotrypsin inhibitor 2 using molecular dynamics: comparison to x-ray crystallographic and NMR data.
Protein Eng. 1995 Nov;8(11):1117-28
Authors: Li A, Daggett V
The native solution structure and dynamics of chymotrypsin inhibitor 2 (CI2) have been studied using a long (5.3 ns) molecular dynamics (MD) simulation without any imposed restraints. The majority of the experimentally observed spin-spin coupling constants, short- and long-range nuclear Overhauser effect (NOE) cross peaks and the amide hydrogen exchange behavior were reproduced by the MD simulation. This good correspondence suggests that the major structural features of the protein during the simulation are representative of the true protein structure in solution. Two water molecules formed hydrogen bond bridges between beta2 and beta3, in agreement with X-ray crystallographic data and a recent reassessment of the solution structure using time-averaged NMR restraints during MD refinement. The active-site loop of the protein displayed the greatest structural changes and the highest mobility. When this loop region was excluded, the average Calpha r.m.s. deviation of the simulated solution structures from the crystal structure was approximately 1.5 Angstrom from 0.5 to 5.3 ns. There is structural heterogeneity in particular regions of the NMR-derived solution structures, which could be a result of imprecision or true internal motion. A study of the distribution of mobility through the protein allows us to distinguish between these two alternatives. In particular, deviations in the active-site loop appear to be a result of heightened mobility, which is also supported by good correspondence between calculated and experimental S2 N-H order parameters. On the other hand, other ill-defined regions of the NMR-derived structures are well defined in the simulation and are probably the result of a lack of structural restraints (i.e. NOEs), as opposed to reflecting the true mobility.
[NMR paper] NMR solution structure of ATTp, an Arabidopsis thaliana trypsin inhibitor.
NMR solution structure of ATTp, an Arabidopsis thaliana trypsin inhibitor.
Related Articles NMR solution structure of ATTp, an Arabidopsis thaliana trypsin inhibitor.
Biochemistry. 2002 Oct 15;41(41):12284-96
Authors: Zhao Q, Chae YK, Markley JL
The three-dimensional structure of the precursor form of the Arabidopsis thaliana trypsin inhibitor (ATT(p), GenBank entry Z46816), a 68-residue (approximately 7.5 kDa) rapeseed class proteinase inhibitor, has been determined in solution at pH 5.0 and 25 degrees C by multinuclear magnetic resonance...
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[NMR paper] Solution NMR structure of the myosin phosphatase inhibitor protein CPI-17 shows phosp
Solution NMR structure of the myosin phosphatase inhibitor protein CPI-17 shows phosphorylation-induced conformational changes responsible for activation.
Related Articles Solution NMR structure of the myosin phosphatase inhibitor protein CPI-17 shows phosphorylation-induced conformational changes responsible for activation.
J Mol Biol. 2001 Dec 7;314(4):839-49
Authors: Ohki S, Eto M, Kariya E, Hayano T, Hayashi Y, Yazawa M, Brautigan D, Kainosho M
Contractility of vascular smooth muscle depends on phosphorylation of myosin light chains, and...
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[NMR paper] NMR solution structure of Apis mellifera chymotrypsin/cathepsin G inhibitor-1 (AMCI-1
NMR solution structure of Apis mellifera chymotrypsin/cathepsin G inhibitor-1 (AMCI-1): structural similarity with Ascaris protease inhibitors.
Related Articles NMR solution structure of Apis mellifera chymotrypsin/cathepsin G inhibitor-1 (AMCI-1): structural similarity with Ascaris protease inhibitors.
Protein Sci. 2000 May;9(5):976-84
Authors: Cierpicki T, Bania J, Otlewski J
The three-dimensional structure of the 56 residue polypeptide Apis mellifera chymotrypsin/cathepsin G inhibitor 1 (AMCI-1) isolated from honey bee hemolymph was...
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[NMR paper] Real-time NMR studies on folding of mutants of barnase and chymotrypsin inhibitor 2.
Real-time NMR studies on folding of mutants of barnase and chymotrypsin inhibitor 2.
Related Articles Real-time NMR studies on folding of mutants of barnase and chymotrypsin inhibitor 2.
FEBS Lett. 1998 Feb 13;423(1):110-2
Authors: Killick TR, Freund SM, Fersht AR
The folding and unfolding of proteins is generally assumed to be so co-operative that the overall process may be followed by a single probe, such as tryptophan fluorescence. Folding kinetics of three mutants of barnase and chymotrypsin inhibitor 2 (CI2) were studied by real-time NMR....
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[NMR paper] Solution structure of synthetic peptide inhibitor and substrate of cAMP-dependent pro
Solution structure of synthetic peptide inhibitor and substrate of cAMP-dependent protein kinase. A study by 2D H NMR and molecular dynamics.
Related Articles Solution structure of synthetic peptide inhibitor and substrate of cAMP-dependent protein kinase. A study by 2D H NMR and molecular dynamics.
J Pept Res. 1997 Mar;49(3):210-20
Authors: Padilla A, Hauer JA, Tsigelny I, Parello J, Taylor SS
Peptides derived from the inhibitor of cAMP-dependent protein kinase. PKI, have been studied by 2D 1H NMR techniques. These include the inhibitor...
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[NMR paper] 1H NMR investigation of the electronic and molecular structure of the four-iron clust
1H NMR investigation of the electronic and molecular structure of the four-iron cluster ferredoxin from the hyperthermophile Pyrococcus furiosus. Identification of Asp 14 as a cluster ligand in each of the four redox states.
Related Articles 1H NMR investigation of the electronic and molecular structure of the four-iron cluster ferredoxin from the hyperthermophile Pyrococcus furiosus. Identification of Asp 14 as a cluster ligand in each of the four redox states.
Biochemistry. 1995 Sep 12;34(36):11373-84
Authors: Calzolai L, Gorst CM, Zhao ZH, Teng Q,...
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[NMR paper] Three-dimensional solution structure of Cucurbita maxima trypsin inhibitor-V determin
Three-dimensional solution structure of Cucurbita maxima trypsin inhibitor-V determined by NMR spectroscopy.
Related Articles Three-dimensional solution structure of Cucurbita maxima trypsin inhibitor-V determined by NMR spectroscopy.
Biochemistry. 1995 Apr 18;34(15):5201-11
Authors: Cai M, Gong Y, Kao JL, Krishnamoorthi R
The solution structure of Cucurbita maxima trypsin inhibitor-V (CMTI-V), which is also a specific inhibitor of the blood coagulation protein, factor XIIa, was determined by 1H NMR spectroscopy in combination with a...
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[NMR paper] The three-dimensional solution structure by 1H NMR of a 6-kDa proteinase inhibitor is
The three-dimensional solution structure by 1H NMR of a 6-kDa proteinase inhibitor isolated from the stigma of Nicotiana alata.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles The three-dimensional solution structure by 1H NMR of a 6-kDa proteinase inhibitor isolated from the stigma of Nicotiana alata.
J Mol Biol. 1994 Sep 23;242(3):231-43
Authors: Nielsen KJ, Heath RL, Anderson MA, Craik DJ
The three-dimensional structure and disulfide connectivities of a 6-kDa...
Investigation of the solution structure of chymotrypsin inhibitor 2 using molecular d
Linear Mode
