Infrared study of the stability and folding kinetics of a 15-residue beta-hairpin.
about
His26 protonation in cytochrome c triggers microsecond β-sheet formation and heme exposure: implications for apoptosisAzidohomoalanine: a conformationally sensitive IR probe of protein folding, protein structure, and electrostatics.Measuring the refolding of beta-sheets with different turn sequences on a nanosecond time scale.Spectroscopic studies of protein folding: linear and nonlinear methodsThe effect of charge-charge interactions on the kinetics of alpha-helix formation.Stability and folding dynamics of polyglutamic acid.Structured pathway across the transition state for peptide folding revealed by molecular dynamics simulationsThe interplay of turn formation and hydrophobic interactions on the early kinetic events in protein folding.Infrared study of the stability and folding kinetics of a series of β-hairpin peptides with a common NPDG turn.Hairpin folding rates reflect mutations within and remote from the turn region.Raising the speed limit for β-hairpin formation.Early turn formation and chain collapse drive fast folding of the major cold shock protein CspA of Escherichia coli.Power-law dependence of the melting temperature of ubiquitin on the volume fraction of macromolecular crowders.Molecular origin of Gerstmann-Sträussler-Scheinker syndrome: insight from computer simulation of an amyloidogenic prion peptide.Achieving secondary structural resolution in kinetic measurements of protein folding: a case study of the folding mechanism of Trp-cage.Dehydration-driven solvent exposure of hydrophobic surfaces as a driving force in peptide foldingUnderstanding the key factors that control the rate of beta-hairpin folding.Light-Switchable Peptides with a Hemithioindigo Unit: Peptide Design, Photochromism, and Optical Spectroscopy.Coarse kMC-based replica exchange algorithms for the accelerated simulation of protein folding in explicit solvent.Molecular dynamics analysis of the conformations of a beta-hairpin miniprotein.Micelle-Triggered β-Hairpin to α-Helix Transition in a 14-Residue Peptide from a Choline-Binding Repeat of the Pneumococcal Autolysin LytAA kMC-MD method with generalized move-sets for the simulation of folding of α-helical and β-stranded peptides.VCD spectroscopic properties of the beta-hairpin forming miniprotein CLN025 in various solvents.Directly monitor protein rearrangement on a nanosecond-to-millisecond time-scale.The CLN025 decapeptide retains a β-hairpin conformation in urea and guanidinium chloride.Modeling the mechanism of CLN025 beta-hairpin formation.An adaptive bias - hybrid MD/kMC algorithm for protein folding and aggregation.Protein folding kinetics and thermodynamics from atomistic simulations.All-atom level direct folding simulation of a betabetaalpha miniprotein.Folding 19 proteins to their native state and stability of large proteins from a coarse-grained model.Impact ofβ-Turn Sequence onβ-Hairpin Dynamics Studied with Infrared-Detected Temperature Jump
P2860
Q28392280-DFEC42EA-D77F-4CAB-ACE7-0A381E9DCFFDQ30393283-DF731231-FF45-4F62-9674-7B4B476C17BFQ30500733-CDF22F57-7A79-4D79-BEA5-28149FA77562Q31042100-8739F356-E281-4F55-93E5-A6A761651E3DQ33294390-74DD1FF8-2717-4968-9114-2CFE0EFCC5B6Q33806048-0F4D68F5-0459-43C9-BAFB-2B4CF843585CQ34022990-18D696D5-A0B4-4429-AF19-16DF71A038D0Q34067088-3461BCFD-42BD-4473-B903-3FC3763643BBQ34089497-C973A049-9490-4C81-8E43-40C5CFFCF81BQ34098386-B2C4107E-37BF-4D4F-AC4F-6748D3B8BCB3Q34371064-75C5CB7D-9B39-45BA-A913-C21C72DD1ECDQ34457824-1E428CB8-F520-4776-A83D-E4ADF2F5DB28Q34722836-97D5BF7A-5E48-45B7-9787-72502742F5BFQ35070483-A4BADC51-9DC4-4881-BBE9-4F7AD9919DADQ35902392-5F767DAC-F723-4222-98A6-CB8376A09E66Q36024304-C8CCB219-6690-4F1B-93FE-CEA874D902E7Q37619359-BBC64F36-3027-4001-931C-10BAE17CB991Q38704077-1C3C854B-A9DC-4965-8CC8-E0011A86B3CEQ39824793-C9BDCFB5-1FA6-43F3-A046-1BE7E5DFA451Q39872354-3B700C8E-A771-4AA5-A071-22181FBC5050Q41008248-802B296A-67A2-4E09-9DAD-ECB56AE4298AQ41068250-A518EACC-C9A9-40F8-9CA1-3AE91D5F17E9Q41108107-872561AE-9E68-4FB9-B0B4-B0C3107702D9Q41460168-BA23D11C-E197-4041-9EC1-9D0EA6C4495AQ42102948-A2CE3205-51B5-492E-8517-E08EF5F012A7Q46259319-EA69001E-9458-4C7E-8CE7-509E8E368030Q47788250-4F4E6CE4-E409-4B6A-B5CF-A597817B38ABQ51630056-8926A11D-87BB-4BE1-8A88-395FCDB94E7FQ51890815-434A9172-6B1F-44E7-ADBF-9C204BBC3F56Q54784061-7F5025C4-0C77-40F5-9C74-9D81E65B632DQ58911153-A10E5783-B959-46AF-AB5E-6724E8E14D65
P2860
Infrared study of the stability and folding kinetics of a 15-residue beta-hairpin.
description
2003 nî lūn-bûn
@nan
2003 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Infrared study of the stability and folding kinetics of a 15-residue beta-hairpin.
@ast
Infrared study of the stability and folding kinetics of a 15-residue beta-hairpin.
@en
type
label
Infrared study of the stability and folding kinetics of a 15-residue beta-hairpin.
@ast
Infrared study of the stability and folding kinetics of a 15-residue beta-hairpin.
@en
prefLabel
Infrared study of the stability and folding kinetics of a 15-residue beta-hairpin.
@ast
Infrared study of the stability and folding kinetics of a 15-residue beta-hairpin.
@en
P2093
P356
P1476
Infrared study of the stability and folding kinetics of a 15-residue beta-hairpin.
@en
P2093
P304
15388-15394
P356
10.1021/JA037053B
P407
P577
2003-12-01T00:00:00Z