Partially folded conformation of the (30-51) intermediate in the disulphide folding pathway of bovine pancreatic trypsin inhibitor. 1H and 15N resonance assignments and determination of backbone dynamics from 15N relaxation measurements.
about
Structure of a protein in a kinetic trapFormation of a native-like subdomain in a partially folded intermediate of bovine pancreatic trypsin inhibitorCharacterization of the structure and dynamics of a near-native equilibrium intermediate in the unfolding pathway of an all beta-barrel protein.Hydrogen exchange in BPTI variants that do not share a common disulfide bond.Characterisation of disulfide-bond dynamics in non-native states of lysozyme and its disulfide deletion mutants by NMR.NMR characterization of partially folded and unfolded conformational ensembles of proteins.Mutational analysis of the BPTI folding pathway: I. Effects of aromatic-->leucine substitutions on the distribution of folding intermediatesMutational analysis of the BPTI folding pathway: II. Effects of aromatic-->leucine substitutions on folding kinetics and thermodynamicsEarly events in the disulfide-coupled folding of BPTI.Structural and dynamic characterization of an unfolded state of poplar apo-plastocyanin formed under nondenaturing conditions.Protein folding coupled to disulphide bond formation.Protein disulfide-isomerase interacts with a substrate protein at all stages along its folding pathway.The equilibrium unfolding of Azotobacter vinelandii apoflavodoxin II occurs via a relatively stable folding intermediateGenetic selection for enhanced folding in vivo targets the Cys14-Cys38 disulfide bond in bovine pancreatic trypsin inhibitor.Apoflavodoxin (un)folding followed at the residue level by NMR.Propensities for the formation of individual disulfide bonds in hen lysozyme and in the size and stability of disulfide-associated submolecular structures.Partially folded structure of monomeric bovine β-lactoglobulinCircular Dichroism of Proteins in Solution and at Interfaces
P2860
Q27730230-68CA772E-55DA-42EF-A1D8-08201EA472A9Q28756235-6D74182F-96D4-4A87-8506-30AA24DBCB16Q30165215-5B3008D9-99A3-4185-B46F-9EDB654747F3Q30416869-67A2DDE9-BCD0-4D1A-B525-1A9597A2D0FFQ31002748-68238019-30FC-4246-BB94-F252490DDFE0Q33749441-4C6439E8-1FEE-4713-A007-24FDC2558E8BQ36280455-FAB182FC-60A7-49C3-BF2E-DB3035BC1DA7Q36280506-84D6D98F-195C-4F05-88F3-70D12F199B86Q36281623-461A3678-A75F-409C-8367-0511E19E3141Q36640705-D1C8D66E-8A96-44BA-8434-73B951FCE6F0Q41648380-5B52F249-BDFC-4EED-B5B6-5F1B273282C8Q41880177-792B5AFB-76F0-4385-AC1D-56E095966D0EQ42174587-8384982E-2C7E-4E89-BCF6-3AE10AFC4DFAQ42627750-7EA10484-7ABC-4250-93E8-78822FF0AE19Q42847317-DC6241BB-1A8D-447F-955C-D1AE916D76BFQ47227351-1AC9A6FC-9AB8-4DA8-A145-69361575B77BQ57591560-9968041A-3B7B-4A39-B3AF-74269D1558D7Q57830260-B01D3483-78BC-4F34-BD0F-12B389BDF9DE
P2860
Partially folded conformation of the (30-51) intermediate in the disulphide folding pathway of bovine pancreatic trypsin inhibitor. 1H and 15N resonance assignments and determination of backbone dynamics from 15N relaxation measurements.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年学术文章
@wuu
1993年学术文章
@zh
1993年学术文章
@zh-cn
1993年学术文章
@zh-hans
1993年学术文章
@zh-my
1993年学术文章
@zh-sg
1993年學術文章
@yue
1993年學術文章
@zh-hant
name
Partially folded conformation ...... m 15N relaxation measurements.
@en
Partially folded conformation of the
@nl
type
label
Partially folded conformation ...... m 15N relaxation measurements.
@en
Partially folded conformation of the
@nl
prefLabel
Partially folded conformation ...... m 15N relaxation measurements.
@en
Partially folded conformation of the
@nl
P2093
P356
P1476
Partially folded conformation ...... om 15N relaxation measurements
@en
P2093
P304
P356
10.1006/JMBI.1993.1108
P407
P577
1993-02-01T00:00:00Z