Disulfide Bond Isomerization in Basic Pancreatic Trypsin Inhibitor:  Multisite Chemical Exchange Quantified by CPMG Relaxation Dispersion and Chemical Shift Modeling

2003 ◽  
Vol 125 (47) ◽  
pp. 14324-14335 ◽  
Author(s):  
Michael J. Grey ◽  
Chunyu Wang ◽  
Arthur G. Palmer
Keyword(s):  
Chemical Shift ◽  
Disulfide Bond ◽  
Trypsin Inhibitor ◽  
Chemical Exchange ◽  
Relaxation Dispersion ◽  
Basic Pancreatic Trypsin Inhibitor ◽  
Pancreatic Trypsin Inhibitor ◽  
Cpmg Relaxation Dispersion ◽  
Disulfide Bond Isomerization

13C-NMR studies on disulfide bond isomerization in bovine pancreatic trypsin inhibitor (BPTI)

2016 ◽  
Vol 66 (1) ◽  
pp. 37-53 ◽  
Author(s):  
Mitsuhiro Takeda ◽  
Yohei Miyanoiri ◽  
Tsutomu Terauchi ◽  
Masatsune Kainosho
Keyword(s):  
Disulfide Bond ◽  
Trypsin Inhibitor ◽  
13C Nmr ◽  
Bovine Pancreatic Trypsin Inhibitor ◽  
Nmr Studies ◽  
Pancreatic Trypsin Inhibitor ◽  
Disulfide Bond Isomerization

scholarly journals 1H NMR Chemical Shift Calculation of .ALPHA.-CH and NH Protons in Basic Pancreatic Trypsin Inhibitor.

1992 ◽  
Vol 49 (4) ◽  
pp. 281-287
Author(s):  
Tetsuo ASAKURA ◽  
Makoto DEMURA ◽  
Eiji NAKAMURA ◽  
Isao ANDO
Keyword(s):  
Chemical Shift ◽  
1H Nmr ◽  
Trypsin Inhibitor ◽  
Nmr Chemical Shift ◽  
Basic Pancreatic Trypsin Inhibitor ◽  
Pancreatic Trypsin Inhibitor ◽  
Shift Calculation ◽  
1H Nmr Chemical Shift

Binding of the bovine basic pancreatic trypsin inhibitor (Kunitz) to human Lys77-plasmin

1986 ◽  
Vol 191 (2) ◽  
pp. 295-297 ◽  
Author(s):  
Enea Menegatti ◽  
Mario Guarneri ◽  
Martino Bolognesi ◽  
Paolo Ascenzi ◽  
Gino Amiconi
Keyword(s):  
Trypsin Inhibitor ◽  
Basic Pancreatic Trypsin Inhibitor ◽  
Pancreatic Trypsin Inhibitor

scholarly journals Screening for Stable Mutants with Amino Acid Pairs Substituted for the Disulfide Bond between Residues 14 and 38 of Bovine Pancreatic Trypsin Inhibitor (BPTI)

2002 ◽  
Vol 277 (52) ◽  
pp. 51043-51048 ◽  
Author(s):  
Yoshihisa Hagihara ◽  
Kentaro Shiraki ◽  
Tsutomu Nakamura ◽  
Koichi Uegaki ◽  
Masahiro Takagi ◽  
...  
Keyword(s):  
Amino Acid ◽  
Disulfide Bond ◽  
Trypsin Inhibitor ◽  
Bovine Pancreatic Trypsin Inhibitor ◽  
Pancreatic Trypsin Inhibitor

scholarly journals Free Energy Landscape and Rate Estimation of the Aromatic Ring Flips in Basic Pancreatic Trypsin Inhibitor Using Metadynamics

2021 ◽  
Author(s):  
Pär Söderhjelm ◽  
Mandar Kulkarni
Keyword(s):  
Free Energy ◽  
Trypsin Inhibitor ◽  
Side Chain ◽  
Side Chains ◽  
Aromatic Residues ◽  
Basic Pancreatic Trypsin Inhibitor ◽  
Pancreatic Trypsin Inhibitor ◽  
Energy Surfaces ◽  
Aromatic Side Chains

Aromatic side-chains (phenylalanine and tyrosine) of a protein flip by 180° around the Cβ-Cγ axis (χ2 dihedral of side-chain) producing two symmetry-equivalent states. The ring-flip dynamics act as an NMR probe to understand local conformational fluctuations. Ring-flips are categorized as slow (ms onwards) or fast (ns to near ms) based on timescales accessible to NMR experiments. In this study, we investigated the ability of the infrequent metadynamics approach to discriminate between slow and fast ring-flips for eight individual aromatic side-chains (F4, Y10, Y21, F22, Y23, F33, Y35, F45) of basic pancreatic trypsin inhibitor (BPTI). Well-tempered metadynamics simulations were performed to observe ring-flipping free energy surfaces for all eight aromatic residues. The results indicate that χ2 as a standalone collective variable (CV) is not sufficient to classify fast and slow ring-flips. Most of the residues needed χ1 (N−Cχα) as a complementary CV, indicating the importance of librational motions in ring-flips. Multiple pathways and mechanisms were observed for residues F4, Y10, and F22. Recrossing events are observed for residues F22 and F33, indicating a possible role of friction effects in the ring-flipping. The results demonstrate the successful application of the metadynamics based approach to estimate ring-flip rates of aromatic residues in BPTI and identify certain limitations of the approach.

Selection of potent chymotrypsin and elastase inhibitors from M13 phage library of basic pancreatic trypsin inhibitor (BPTI)

2001 ◽  
Vol 1550 (2) ◽  
pp. 153-163 ◽  
Author(s):  
Liliana Kiczak ◽  
Monika Kasztura ◽  
Katarzyna Koscielska-Kasprzak ◽  
Michal Dadlez ◽  
Jacek Otlewski
Keyword(s):  
Trypsin Inhibitor ◽  
Phage Library ◽  
Basic Pancreatic Trypsin Inhibitor ◽  
Pancreatic Trypsin Inhibitor ◽  
M13 Phage ◽  
Selection Of
Sign in / Sign up

Export Citation Format

Share Document