Yusuf Hamied Department of Chemistry

Publications

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  • Currently displaying 22141 - 22160 of 29681 publications
Author(s)
Publication title
Journal Name
Publication year
NMR studies of the dynamics of the multidomain protein urokinase-type plasminogen activator
UK Nowak, X Li, AJ Teuten, RA Smith, CM Dobson
Biochemistry
(2002)
32
(doi: 10.1021/bi00052a038)
Folding of subtilisin BPN': characterization of a folding intermediate
J Eder, M Rheinnecker, AR Fersht
Biochemistry
(2002)
32
(doi: 10.1021/bi00052a004)
Conversion of Cytochrome b562 to c-Type Cytochromes
PD Barker, EP Nerou, SM Freund, IM Fearnley
Biochemistry
(2002)
34
(doi: 10.1021/bi00046a027)
Nature and Consequences of GroEL-Protein Interactions
LS Itzhaki, DE Otzen, AR Fersht
Biochemistry
(2002)
34
(doi: 10.1021/bi00044a037)
Movement of the Position of the Transition State in Protein Folding
A Matouschek, DE Otzen, LS Itzhaki, SE Jackson, AR Fersht
Biochemistry
(2002)
34
(doi: 10.1021/bi00041a047)
Characterization of Conformational Preferences in a Partly Folded Protein by Heteronuclear NMR Spectroscopy: Assignment and Secondary Structure Analysis of Hen Egg-White Lysozyme in Trifluoroethanol
M Buck, H Schwalbe, CM Dobson
Biochemistry
(2002)
34
(doi: 10.1021/bi00040a038)
STRUCTURAL FACTORS CONTRIBUTING TO THE HYDROPHOBIC EFFECT - THE PARTLY EXPOSED HYDROPHOBIC MINICORE IN CHYMOTRYPSIN INHIBITOR-2
DE Otzen, M Rheinnecker, AR Fersht
Biochemistry
(2002)
34
(doi: 10.1021/bi00040a016)
Comparison of MD Simulations and NMR Experiments for Hen Lysozyme. Analysis of Local Fluctuations, Cooperative Motions, and Global Changes
LJ Smith, AE Mark, CM Dobson, WF van Gunsteren
Biochemistry
(2002)
34
(doi: 10.1021/bi00034a026)
pKA values of carboxyl groups in the native and denatured states of barnase: the pKA values of the denatured state are on average 0.4 units lower than those of model compounds.
M Oliveberg, VL Arcus, AR Fersht
Biochemistry
(2002)
34
(doi: 10.1021/bi00029a018)
Relationship between Equilibrium Amide Proton Exchange Behavior and the Folding Pathway of Bamase
S Perrett, J Clarke, AM Hounslow, AR Fersht
Biochemistry
(2002)
34
(doi: 10.1021/bi00029a003)
Peptide aldehyde inhibitors of hepatitis A virus 3C proteinase.
BA Malcolm, C Lowe, S Shechosky, RT McKay, CC Yang, VJ Shah, RJ Simon, JC Vederas, DV Santi
Biochemistry
(2002)
34
(doi: 10.1021/bi00025a024)
Mechanism of metal-independent hydroxylation by Chromobacterium violaceum phenylalanine hydroxylase.
RT Carr, S Balasubramanian, PC Hawkins, SJ Benkovic
Biochemistry
(2002)
34
(doi: 10.1021/bi00022a028)
FOLDING OF A 4-HELIX BUNDLE - STUDIES OF ACYL-COENZYME-A BINDING-PROTEIN
BB Kragelund, CV Robinson, J Knudsen, CM Dobson, FM Poulsen
Biochemistry
(2002)
34
(doi: 10.1021/bi00021a037)
Mechanism of chymotrypsin. Structure, reactivity, and nonproductive binding relations
J Fastrez, AR Fersht
Biochemistry
(2002)
12
(doi: 10.1021/bi00730a008)
Formaldehyde metabolism by Escherichia coli. Carbon and solvent deuterium incorporation into glycerol, 1,2-propanediol, and 1,3-propanediol.
BK Hunter, KM Nicholls, JK Sanders
Biochemistry
(2002)
24
(doi: 10.1021/bi00336a050)
Conformations of two duplex forms of d(TCGA) in slow-exchange equilibrium characterized by NMR
DG Reid, SA Salisbury, T Brown, DH Williams
Biochemistry
(2002)
24
(doi: 10.1021/bi00337a011)
Probing histidine-substrate interactions in tyrosyl-tRNA synthetase using asparagine and glutamine replacements.
DM Lowe, AR Fersht, AJ Wilkinson, P Carter, G Winter
Biochemistry
(2002)
24
(doi: 10.1021/bi00340a022)
Reversible dissociation of dimeric tyrosyl-tRNA synthetase by mutagenesis at the subunit interface.
DH Jones, AJ McMillan, AR Fersht, G Winter
Biochemistry
(2002)
24
(doi: 10.1021/bi00342a024)
Fine structure-activity analysis of mutations at position 51 of tyrosyl-tRNA synthetase.
AR Fersht, AJ Wilkinson, P Carter, G Winter
Biochemistry
(2002)
24
(doi: 10.1021/bi00342a025)
Use of binding energy in catalysis analyzed by mutagenesis of the tyrosyl-tRNA synthetase
TN Wells, AR Fersht
Biochemistry
(2002)
25
(doi: 10.1021/bi00356a007)
Yusuf Hamied Department of Chemistry
Lensfield Road
Cambridge
CB2 1EW
T: +44 (0) 1223 336300
enquiries@ch.cam.ac.uk
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