An evaluation of the use of hydrogen exchange at equilibrium to probe intermediates on the protein folding pathway.
about
NMR solution structure of the activation domain of human procarboxypeptidase A2Conformational stability of ribonuclease T1 determined by hydrogen-deuterium exchangeIdentification of compact, hydrophobically stabilized domains and modules containing multiple peptide chainsNMR Studies on Structure and Dynamics of the Monomeric Derivative of BS-RNase: New Insights for 3D Domain SwappingStructural cooperativity in the SH3 domain studied by site-directed mutagenesis and amide hydrogen exchange.Protein folding and misfolding: mechanism and principles.Mapping the lifetimes of local opening events in a native state protein.The HD-exchange motions of ribosomal protein S6 are insensitive to reversal of the protein-folding pathway.Microscopic stability of cold shock protein A examined by NMR native state hydrogen exchange as a function of urea and trimethylamine N-oxideA quantitative, high-throughput screen for protein stability.Thermodynamic stability measurements on multimeric proteins using a new H/D exchange- and matrix-assisted laser desorption/ionization (MALDI) mass spectrometry-based method.The hydrogen exchange core and protein folding.Cytochrome c folding pathway: kinetic native-state hydrogen exchange.OneG: a computational tool for predicting cryptic intermediates in the unfolding kinetics of proteins under native conditionsAn amino acid code for protein foldingStudies of biomolecular conformations and conformational dynamics by mass spectrometry.The propagation of binding interactions to remote sites in proteins: analysis of the binding of the monoclonal antibody D1.3 to lysozymeLipid binding protein response to a bile acid library: a combined NMR and statistical approach.The structural distribution of cooperative interactions in proteins: analysis of the native state ensemblePartially Unfolded Forms of the Prion Protein Populated under Misfolding-promoting Conditions: CHARACTERIZATION BY HYDROGEN EXCHANGE MASS SPECTROMETRY AND NMR.Scope and utility of hydrogen exchange as a tool for mapping landscapesFolding subdomains of thioredoxin characterized by native-state hydrogen exchangeAbsence of stable intermediates on the folding pathway of barnase.Thermodynamic characterization of the unfolding of the prion protein.Mechanism of Protein Denaturation: Partial Unfolding of the P22 Coat Protein I-Domain by Urea Binding.Initial denaturing conditions influence the slow folding phase of acylphosphatase associated with proline isomerization.Functional dynamics of hexameric helicase probed by hydrogen exchange and simulation.Destabilizing mutations alter the hydrogen exchange mechanism in ribonuclease A.Folding intermediates of a model three-helix bundle protein. Pressure and cold denaturation studies.Hydrogen exchange of the tetramerization domain of the human tumour suppressor p53 probed by denaturants and temperature.Influence of pH on the structure and stability of the sweet protein MNEI.The effect of inhibitor binding on the structural stability and cooperativity of the HIV-1 protease.Comparison of the amide proton exchange behavior of the rapidly formed folding intermediate and the native state of an antibody scFv fragment
P2860
Q24649175-EE228D9D-17D5-4A37-AF7D-886DE8AE8860Q24673412-F3247D10-181E-44D5-9E9D-11D1D782BDCDQ24673486-D9CC260B-056D-47EF-B22E-C0C0DC5C22EDQ27676787-812F1211-2B5F-4A0F-9235-21D844652CA6Q30164813-47939AAC-C91D-4466-A6DE-B83C557FB98BQ30368801-4AA6E990-C054-4EFF-AC94-6B0063216DBEQ30432041-CD919669-6927-49B2-96C9-943B48586949Q30492596-3B5318CB-A6F0-453B-98C2-110D216B31B7Q30587207-84E82F05-02A8-425A-9EA1-F1CD8FACA81BQ30885030-32B2CE0F-7B1C-4287-8782-7435F82232F7Q31044556-5422D926-FAA5-4378-A8C8-C07DB4A5E542Q33714720-C73DF57A-847D-4291-AB69-D617D7FDA738Q34155517-2833427E-2A4A-4866-B1BC-3B15C8F2F4BBQ34193156-AB05B726-8400-4F7F-B76D-CC779E727B50Q34584803-3403FDB0-E7A7-40AF-B038-39ACA1115BFAQ34811742-17C6F24F-768A-437C-B0EE-4EFA1C248286Q35616205-2D9E7E67-478D-4772-AA9F-BD5074B9ADD8Q35741925-37C06240-9A66-4720-9A34-2F5A8DA86839Q36279800-9468CF79-9942-4C82-904E-20222C3ADBDAQ36283277-5F3EE51C-3354-4148-82C8-1124B9324AEAQ36398791-7B71B5D3-756C-44B6-9331-B76175468F9CQ36572178-520EDC96-EBB9-4382-8FA2-0EC4CFDE538CQ37260926-3CC23ADD-E8AF-4294-A359-2FB9175B9634Q37533502-7E794D66-69BC-4F21-882D-914CE2C10784Q40196074-8F8D3BF6-B9E0-4507-9B59-702D71BCAF55Q41761688-B8917B05-388F-4301-8D2A-79F9A2DCD508Q41872676-08E32FF7-428C-4387-AC91-ED4ACB71F223Q42029602-1CC42A67-6B41-43CE-9762-16154AA242DAQ43559580-9D2DA6D4-D316-4752-AA14-115BF0D446CDQ43739320-FEB6A677-4D56-49AF-80A3-F3928D676771Q48282757-C9429EA5-B2EC-4517-A04C-CC6D6061A4FEQ52209873-5F1AD1FB-E4FB-46D5-A190-D8233B38A28CQ57840088-9D2500B6-D0F0-467B-A426-348698A36F9C
P2860
An evaluation of the use of hydrogen exchange at equilibrium to probe intermediates on the protein folding pathway.
description
1996 nî lūn-bûn
@nan
1996 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
name
An evaluation of the use of hy ...... n the protein folding pathway.
@ast
An evaluation of the use of hy ...... n the protein folding pathway.
@en
type
label
An evaluation of the use of hy ...... n the protein folding pathway.
@ast
An evaluation of the use of hy ...... n the protein folding pathway.
@en
prefLabel
An evaluation of the use of hy ...... n the protein folding pathway.
@ast
An evaluation of the use of hy ...... n the protein folding pathway.
@en
P1433
P1476
An evaluation of the use of hy ...... n the protein folding pathway.
@en
P2093
P304
P356
10.1016/S1359-0278(96)00038-7
P50
P577
1996-01-01T00:00:00Z