Spectroscopic studies of protein folding: linear and nonlinear methods
about
Kinetics of peptide folding in lipid membranesA molecular interpretation of 2D IR protein folding experiments with Markov state modelsEster carbonyl vibration as a sensitive probe of protein local electric field.Distinguishing unfolding and functional conformational transitions of calmodulin using ultraviolet resonance Raman spectroscopy.Experimental validation of the role of trifluoroethanol as a nanocrowder.Tightening up the structure, lighting up the pathway: Application of molecular constraints and light to manipulate protein folding, self-assembly and function.Structural disorder of folded proteins: isotope-edited 2D IR spectroscopy and Markov state modeling.Sensing pH via p-cyanophenylalanine fluorescence: Application to determine peptide pKa and membrane penetration kinetics.IR-induced conformational isomerization of a helical peptide in a cold ion trap.Probing the Folding-Unfolding Transition of a Thermophilic Protein, MTH1880Using thioamides to site-specifically interrogate the dynamics of hydrogen bond formation in β-sheet folding.Biomolecular Crowding Arising from Small Molecules, Molecular Constraints, Surface Packing, and Nano-Confinement.Dual time-resolved temperature-jump fluorescence and infrared spectroscopy for the study of fast protein dynamics.Interaction Networks in Protein Folding via Atomic-Resolution Experiments and Long-Time-Scale Molecular Dynamics SimulationsThermally induced protein unfolding probed by isotope-edited IR spectroscopy.Solute's perspective on how trimethylamine oxide, urea, and guanidine hydrochloride affect water's hydrogen bonding abilityHow Sensitive is the Amide I Vibration of the Polypeptide Backbone to Electric Fields?Direct measurement of the tryptophan-mediated photocleavage kinetics of a protein disulfide bondQuenching of p-Cyanophenylalanine Fluorescence by Various Anionsα-helix to β-hairpin transition of human amylin monomer.Using VIPT-jump to distinguish between different folding mechanisms: application to BBL and a Trpzip.Infrared and Fluorescence Assessment of Protein Dynamics: From Folding to Function.Meandering Down the Energy Landscape of Protein Folding: Are We There Yet?Using D-Amino Acids to Delineate the Mechanism of Protein Folding: Application to Trp-cage.How quickly can a β-hairpin fold from its transition state?Ultrafast hydrogen exchange reveals specific structural events during the initial stages of folding of cytochrome cNovel microscale approaches for easy, rapid determination of protein stability in academic and commercial settings.Mass spectrometric characterization of protein structures and protein complexes in condensed and gas phase.Microscopic nucleation and propagation rates of an alanine-based α-helix.Simple method to introduce an ester infrared probe into proteins.Coordination to lanthanide ions distorts binding site conformation in calmodulin.Equilibrium versus Nonequilibrium Peptide Dynamics: Insights into Transient 2D IR Spectroscopy
P2860
Q26859563-F10A051D-F484-43AC-AA29-9EB98065181CQ28660159-A7771E32-8805-4EF8-8333-7817ADD826DDQ33925271-34EA0A9D-EDED-476D-BFF2-D09C770EF29FQ33977824-0039DECF-D7E1-4CB1-AD27-A03A85CD2B55Q34281435-9F203F77-453A-45E4-A21E-A5AD7E0361A7Q35111788-7994EFB3-9B03-433F-B6AE-43E25BDFF9A9Q35333283-BAE165EA-DE8F-4336-8D4F-75E6E3343167Q35705907-D9180061-5E8E-4815-B0EF-ED63B3CA637EQ35889301-6A6924DE-7044-450B-8B97-6A6AEF371234Q35893979-A7C9F84E-3074-4569-A26C-8C096E01A4A2Q35965737-DB4CA629-808D-4443-BAC0-ACCE65805A64Q36176612-91BA77EB-0E75-4F6E-8997-C9DC953B25FFQ36277891-3FBE0CB4-8D0C-461A-A076-F098177CA0B5Q36288790-C0F55A48-8187-4976-96C6-9A4129F031FFQ36294499-F97C8874-D45C-4E76-8A15-D51F29A886B1Q36331161-17D91955-6B63-44D0-9D47-20F34A9A60E9Q36470386-90284C9B-B249-44D2-A33F-F7F201672392Q36746404-868B2876-A2FA-42E5-932B-F9C9873DA240Q36807287-D508DDB8-6DA9-4FF6-9269-3C585EC7EBA3Q36815150-D15D0096-CF6B-49B0-97ED-C68B331CF00DQ36996200-5459C8E3-2B19-4046-B72B-D943EA33A420Q37013963-3B900D90-5A45-40AA-B69E-F7562E9C5D14Q37084207-C866DC3D-A248-4E3A-ADB3-CD3CCB5C9294Q37351363-7A5C4166-7A17-4600-8935-93009844CCDFQ37671331-0527FC3A-DEAE-4811-A684-9B9D74D0A91DQ38299234-42839BA0-1011-470D-B4B3-7057DA28DD3AQ43152204-A583E5C2-4540-4F01-8C88-D8C7B794734AQ46219687-2EC92454-DBDE-49E5-94C1-35DC368D2FCDQ48048113-121E1995-5221-4323-AACA-6C04A89194E2Q51344851-C2BFE301-FDAF-41DE-9CA0-1F9841B81EF7Q52353920-DDA1BE55-9CDE-41D2-878C-4C6F38584989Q58788776-C721D731-EE6D-48F6-8A23-4342AC7F22D6
P2860
Spectroscopic studies of protein folding: linear and nonlinear methods
description
2011 nî lūn-bûn
@nan
2011 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Spectroscopic studies of protein folding: linear and nonlinear methods
@ast
Spectroscopic studies of protein folding: linear and nonlinear methods
@en
type
label
Spectroscopic studies of protein folding: linear and nonlinear methods
@ast
Spectroscopic studies of protein folding: linear and nonlinear methods
@en
prefLabel
Spectroscopic studies of protein folding: linear and nonlinear methods
@ast
Spectroscopic studies of protein folding: linear and nonlinear methods
@en
P2093
P2860
P356
P1433
P1476
Spectroscopic studies of protein folding: linear and nonlinear methods
@en
P2093
Arnaldo L Serrano
Matthias M Waegele
P2860
P304
P356
10.1002/PRO.2006
P577
2011-12-28T00:00:00Z