[NMR thesis] Nuclear Magnetic Resonance Studies of ?-Chymotrypsin. I. NMR Studies of the Binding of Small Molecule Inhibitors to ?-Chymotrypsin. II. NMR Studies of the Interaction of N-TFA-D-Tryptophan Semicarbazide with ?-Chymotrypsin. III. ^(13)C-NMR Studies of
Nuclear Magnetic Resonance Studies of ?-Chymotrypsin. I. NMR Studies of the Binding of Small Molecule Inhibitors to ?-Chymotrypsin. II. NMR Studies of the Interaction of N-TFA-D-Tryptophan Semicarbazide with ?-Chymotrypsin. III. ^(13)C-NMR Studies of
Gammon, Kenneth Lee (1973) Nuclear Magnetic Resonance Studies of ?-Chymotrypsin. I. NMR Studies of the Binding of Small Molecule Inhibitors to ?-Chymotrypsin. II. NMR Studies of the Interaction of N-TFA-D-Tryptophan Semicarbazide with ?-Chymotrypsin. III. ^(13)C-NMR Studies of Methylated ?-Chymotrypsin. IV. NMR Studies of Acylated Chymotrypsins. Dissertation (Ph.D.), California Institute of Technology. http://resolver.caltech.edu/CaltechT...2018-102944228
[NMR paper] Interaction of lafutidine in binding to human serum albumin in gastric ulcer therapy: STD-NMR, WaterLOGSY-NMR, NMR relaxation times, Tr-NOESY, molecule docking, and spectroscopic studies.
Interaction of lafutidine in binding to human serum albumin in gastric ulcer therapy: STD-NMR, WaterLOGSY-NMR, NMR relaxation times, Tr-NOESY, molecule docking, and spectroscopic studies.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Interaction of lafutidine in binding to human serum albumin in gastric ulcer therapy: STD-NMR, WaterLOGSY-NMR, NMR relaxation times, Tr-NOESY, molecule docking, and spectroscopic studies.
Arch Biochem Biophys. 2016 Sep 15;606:81-9
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[NMR paper] NMR and MD Studies Reveal That the Isolated Dengue NS3 Protease Is an Intrinsically Disordered Chymotrypsin Fold Which Absolutely Requests NS2B for Correct Folding and Functional Dynamics.
NMR and MD Studies Reveal That the Isolated Dengue NS3 Protease Is an Intrinsically Disordered Chymotrypsin Fold Which Absolutely Requests NS2B for Correct Folding and Functional Dynamics.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.plosone.org-images-pone_120x30.png http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.ncbi.nlm.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles NMR and MD Studies Reveal That the Isolated Dengue NS3 Protease Is an Intrinsically Disordered Chymotrypsin Fold Which Absolutely Requests...
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05-24-2016 11:36 AM
[NMR paper] NMR Solution Structure of a Chymotrypsin Inhibitor from the Taiwan Cobra Naja naja atra.
NMR Solution Structure of a Chymotrypsin Inhibitor from the Taiwan Cobra Naja naja atra.
NMR Solution Structure of a Chymotrypsin Inhibitor from the Taiwan Cobra Naja naja atra.
Molecules. 2013;18(8):8906-8918
Authors: Lin YJ, Ikeya T, Güntert P, Chang LS
Abstract
The Taiwan cobra (Naja naja atra) chymotrypsin inhibitor (NACI) consists of 57 amino acids and is related to other Kunitz-type inhibitors such as bovine pancreatic trypsin inhibitor (BPTI) and Bungarus fasciatus fraction IX (BF9), another chymotrypsin inhibitor. Here we present...
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07-31-2013 12:00 PM
Preparation of protein samples for NMR structure, function, and small-molecule screening studies.
Preparation of protein samples for NMR structure, function, and small-molecule screening studies.
Preparation of protein samples for NMR structure, function, and small-molecule screening studies.
Methods Enzymol. 2011;493:21-60
Authors: Acton TB, Xiao R, Anderson S, Aramini J, Buchwald WA, Ciccosanti C, Conover K, Everett J, Hamilton K, Huang YJ, Janjua H, Kornhaber G, Lau J, Lee DY, Liu G, Maglaqui M, Ma L, Mao L, Patel D, Rossi P, Sahdev S, Shastry R, Swapna GV, Tang Y, Tong S, Wang D, Wang H, Zhao L, Montelione GT
In this chapter, we...
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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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11-18-2010 09:15 PM
[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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11-17-2010 11:06 PM
[NMR paper] Investigation of the solution structure of chymotrypsin inhibitor 2 using molecular d
Investigation of the solution structure of chymotrypsin inhibitor 2 using molecular dynamics: comparison to x-ray crystallographic and NMR data.
Related Articles Investigation 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...
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08-22-2010 03:50 AM
[NMR paper] 13C NMR study of the effects of mutation on the tryptophan dynamics in chymotrypsin i
13C NMR study of the effects of mutation on the tryptophan dynamics in chymotrypsin inhibitor 2: correlations with structure and stability.
Related Articles 13C NMR study of the effects of mutation on the tryptophan dynamics in chymotrypsin inhibitor 2: correlations with structure and stability.
Biochemistry. 1993 Jan 19;32(2):657-62
Authors: Matthews SJ, Jandu SK, Leatherbarrow RJ
Recombinant chymotrypsin inhibitor 2 (CI-2) and the three mutants Ile39-->Val, Ile39-->Leu, and Arg67-->Ala were successfully enriched with tryptophan at position...